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P28352

- APEX1_MOUSE

UniProt

P28352 - APEX1_MOUSE

Protein

DNA-(apurinic or apyrimidinic site) lyase

Gene

Apex1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA.2 Publications

    Catalytic activityi

    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.PROSITE-ProRule annotation

    Cofactori

    Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.By similarity

    Enzyme regulationi

    NPM1 stimulates endodeoxyribonuclease activity on double-stranded DNA with AP sites, but inhibits endoribonuclease activity on single-stranded RNA containing AP sites.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei30 – 312Cleavage; by granzyme ABy similarity
    Metal bindingi69 – 691Magnesium 1By similarity
    Metal bindingi95 – 951Magnesium 1By similarity
    Active sitei170 – 1701By similarity
    Active sitei209 – 2091Proton donor/acceptorBy similarity
    Metal bindingi209 – 2091Magnesium 2By similarity
    Metal bindingi211 – 2111Magnesium 2By similarity
    Sitei211 – 2111Important for substrate recognitionBy similarity
    Sitei211 – 2111Transition state stabilizerBy similarity
    Sitei282 – 2821Important for catalytic activityBy similarity
    Metal bindingi307 – 3071Magnesium 1By similarity
    Sitei308 – 3081Interaction with DNA substrateBy similarity

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. chromatin DNA binding Source: UniProtKB
    3. damaged DNA binding Source: UniProtKB
    4. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
    5. DNA binding Source: UniProtKB
    6. double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: RefGenome
    7. endoribonuclease activity Source: Ensembl
    8. metal ion binding Source: UniProtKB
    9. oxidoreductase activity Source: UniProtKB
    10. phosphoric diester hydrolase activity Source: Ensembl
    11. RNA binding Source: UniProtKB-KW
    12. site-specific endodeoxyribonuclease activity, specific for altered base Source: UniProtKB
    13. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. base-excision repair Source: RefGenome
    3. cell redox homeostasis Source: MGI
    4. cellular response to cAMP Source: Ensembl
    5. cellular response to hydrogen peroxide Source: Ensembl
    6. cellular response to peptide hormone stimulus Source: Ensembl
    7. DNA catabolic process, endonucleolytic Source: GOC
    8. DNA catabolic process, exonucleolytic Source: GOC
    9. DNA demethylation Source: UniProtKB
    10. DNA recombination Source: UniProtKB-KW
    11. DNA repair Source: UniProtKB
    12. negative regulation of smooth muscle cell migration Source: Ensembl
    13. nucleic acid phosphodiester bond hydrolysis Source: GOC
    14. positive regulation of DNA repair Source: UniProtKB
    15. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
    16. regulation of mRNA stability Source: UniProtKB
    17. regulation of transcription, DNA-templated Source: UniProtKB-KW
    18. response to drug Source: Ensembl
    19. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Endonuclease, Exonuclease, Hydrolase, Lyase, Nuclease, Repressor

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_219337. Removal of DNA patch containing abasic residue.
    REACT_219627. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.
    REACT_220827. Displacement of DNA glycosylase by APE1.
    REACT_227394. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase (EC:3.1.-.-, EC:4.2.99.18)
    Alternative name(s):
    APEX nuclease
    Short name:
    APEN
    Apurinic-apyrimidinic endonuclease 1
    Short name:
    AP endonuclease 1
    REF-1
    Redox factor-1
    Cleaved into the following chain:
    Gene namesi
    Name:Apex1
    Synonyms:Ape, Apex, Ref1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:88042. Apex1.

    Subcellular locationi

    Nucleus. Nucleusnucleolus By similarity. Nucleus speckle PROSITE-ProRule annotation. Endoplasmic reticulum By similarity. Cytoplasm
    Note: Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 63-79). S-nitrosylation at Cys-92 and Cys-309 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch By similarity.By similarity
    Chain DNA-(apurinic or apyrimidinic site) lyase, mitochondrial : Mitochondrion
    Note: Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress By similarity. The cleaved APEX2 is only detected in mitochondria.By similarity

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: MGI
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. mitochondrion Source: UniProtKB
    5. nuclear speck Source: UniProtKB
    6. nucleolus Source: UniProtKB
    7. nucleoplasm Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531S → A: Reduced CDK5-mediated phosphorylation. Loss of CDK5-mediated phosphorylation; when associated with T-232.
    Mutagenesisi232 – 2321T → A: Reduced CDK5-mediated phosphorylation. Confers neuron resistance to MPP(+)/MPTP (1-methyl-4-phenylpyridinium). Loss of CDK5-mediated phosphorylation; when associated with S-53. 1 Publication
    Mutagenesisi232 – 2321T → E: Confers neuron sensitivity to MPP(+)/MPTP (1-methyl-4-phenylpyridinium). 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 317316DNA-(apurinic or apyrimidinic site) lyasePRO_0000200011Add
    BLAST
    Chaini31 – 317287DNA-(apurinic or apyrimidinic site) lyase, mitochondrialBy similarityPRO_0000402573Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61N6-acetyllysine; by EP300By similarity
    Modified residuei7 – 71N6-acetyllysine; by EP300By similarity
    Modified residuei26 – 261N6-acetyllysineBy similarity
    Modified residuei30 – 301N6-acetyllysineBy similarity
    Modified residuei31 – 311N6-acetyllysineBy similarity
    Modified residuei34 – 341N6-acetyllysineBy similarity
    Disulfide bondi64 ↔ 92AlternateBy similarity
    Modified residuei64 – 641S-nitrosocysteine; alternateBy similarity
    Modified residuei92 – 921S-nitrosocysteine; alternateBy similarity
    Modified residuei196 – 1961N6-acetyllysineBy similarity
    Modified residuei232 – 2321Phosphothreonine; by CDK51 Publication
    Modified residuei309 – 3091S-nitrosocysteineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation By similarity. Phosphorylation of Thr-232 by CDK5 in response to MPP+/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death.By similarity1 Publication
    Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H2O2 and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 By similarity.By similarity
    Cleaved at Lys-30 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress By similarity.By similarity
    Cys-64 and Cys-92 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES).By similarity
    Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation.By similarity

    Keywords - PTMi

    Acetylation, Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP28352.
    PaxDbiP28352.
    PRIDEiP28352.

    PTM databases

    PhosphoSiteiP28352.

    Expressioni

    Tissue specificityi

    Expressed in both resting and stimulated B cells stimulated to switch (at protein level).

    Gene expression databases

    ArrayExpressiP28352.
    BgeeiP28352.
    CleanExiMM_APEX1.
    GenevestigatoriP28352.

    Interactioni

    Subunit structurei

    Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed of at least APEX1, SET, ANP32A, HMGB2, NME1 and TREX1. Associates with the dimer XRCC5/XRCC6 in a DNA-dependent manner. Interacts with SIRT1; the interaction is increased in the context of genotoxic stress. Interacts with HDAC1, HDAC2 and HDAC3; the interactions are not dependent on the APEX1 acetylation status. Interacts with XRCC1; the interaction is induced by SIRT1 and increased with the APEX1 acetylated form. Interacts with NPM1 (via N-terminal domain); the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts (via N-terminus) with YBX1 (via C-terminus); the interaction is increased in presence of APEX1 acetylated at Lys-6 and Lys-7. Interacts with HNRNPL; the interaction is DNA-dependent. Interacts (via N-terminus) with KPNA1 and KPNA2. Interacts with TXN; the interaction stimulates the FOS/JUN AP-1 complex DNA-binding activity in a redox-dependent manner. Interacts with GZMA, KRT8, MDM2, POLB, PRDX6, PRPF19, RPLP0, TOMM20 and WDR77. Binds to CDK5.1 Publication

    Protein-protein interaction databases

    BioGridi198145. 6 interactions.
    IntActiP28352. 1 interaction.
    MINTiMINT-4088018.
    STRINGi10090.ENSMUSP00000042602.

    Structurei

    3D structure databases

    ProteinModelPortaliP28352.
    SMRiP28352. Positions 43-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 3231Necessary for interaction with YBX1, binding to RNA, association together with NPM1 to rRNA, endoribonuclease activity on abasic RNA and localization in the nucleoliBy similarityAdd
    BLAST
    Regioni8 – 125Nuclear localization signal (NLS)By similarity
    Regioni22 – 3211Necessary for interaction with NPM1 and for efficient rRNA bindingBy similarityAdd
    BLAST
    Regioni63 – 7917Nuclear export signal (NES)By similarityAdd
    BLAST
    Regioni288 – 31730Mitochondrial targeting sequence (MTS)By similarityAdd
    BLAST

    Domaini

    The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins By similarity.By similarity

    Sequence similaritiesi

    Belongs to the DNA repair enzymes AP/ExoA family.Curated

    Phylogenomic databases

    eggNOGiCOG0708.
    HOGENOMiHOG000034586.
    HOVERGENiHBG050531.
    InParanoidiP28352.
    KOiK10771.
    OMAiIEKPSDH.
    OrthoDBiEOG7C8GJ6.
    PhylomeDBiP28352.
    TreeFamiTF315048.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR020848. AP_endonuclease_F1_CS.
    IPR005135. Endo/exonuclease/phosphatase.
    [Graphical view]
    PANTHERiPTHR22748. PTHR22748. 1 hit.
    PfamiPF03372. Exo_endo_phos. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.
    TIGRFAMsiTIGR00633. xth. 1 hit.
    PROSITEiPS00726. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P28352-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRGKKAAA DDGEEPKSEP ETKKSKGAAK KTEKEAAGEG PVLYEDPPDQ    50
    KTSPSGKSAT LKICSWNVDG LRAWIKKKGL DWVKEEAPDI LCLQETKCSE 100
    NKLPAELQEL PGLTHQYWSA PSDKEGYSGV GLLSRQCPLK VSYGIGEEEH 150
    DQEGRVIVAE FESFVLVTAY VPNAGRGLVR LEYRQRWDEA FRKFLKDLAS 200
    RKPLVLCGDL NVAHEEIDLR NPKGNKKNAG FTPQERQGFG ELLQAVPLAD 250
    SFRHLYPNTA YAYTFWTYMM NARSKNVGWR LDYFLLSHSL LPALCDSKIR 300
    SKALGSDHCP ITLYLAL 317
    Length:317
    Mass (Da):35,490
    Last modified:January 23, 2007 - v2
    Checksum:iCF086691FAC89C4A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90374 mRNA. Translation: BAA14382.1.
    U12273 Genomic DNA. Translation: AAC13769.1.
    D38077 Genomic DNA. Translation: BAA07270.1.
    BC052401 mRNA. Translation: AAH52401.1.
    CCDSiCCDS27027.1.
    PIRiA39500.
    RefSeqiNP_033817.1. NM_009687.2.
    XP_006518519.1. XM_006518456.1.
    UniGeneiMm.203.
    Mm.239117.

    Genome annotation databases

    EnsembliENSMUST00000049411; ENSMUSP00000042602; ENSMUSG00000035960.
    GeneIDi11792.
    KEGGimmu:11792.
    UCSCiuc007tly.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90374 mRNA. Translation: BAA14382.1 .
    U12273 Genomic DNA. Translation: AAC13769.1 .
    D38077 Genomic DNA. Translation: BAA07270.1 .
    BC052401 mRNA. Translation: AAH52401.1 .
    CCDSi CCDS27027.1.
    PIRi A39500.
    RefSeqi NP_033817.1. NM_009687.2.
    XP_006518519.1. XM_006518456.1.
    UniGenei Mm.203.
    Mm.239117.

    3D structure databases

    ProteinModelPortali P28352.
    SMRi P28352. Positions 43-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198145. 6 interactions.
    IntActi P28352. 1 interaction.
    MINTi MINT-4088018.
    STRINGi 10090.ENSMUSP00000042602.

    PTM databases

    PhosphoSitei P28352.

    Proteomic databases

    MaxQBi P28352.
    PaxDbi P28352.
    PRIDEi P28352.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049411 ; ENSMUSP00000042602 ; ENSMUSG00000035960 .
    GeneIDi 11792.
    KEGGi mmu:11792.
    UCSCi uc007tly.2. mouse.

    Organism-specific databases

    CTDi 328.
    MGIi MGI:88042. Apex1.

    Phylogenomic databases

    eggNOGi COG0708.
    HOGENOMi HOG000034586.
    HOVERGENi HBG050531.
    InParanoidi P28352.
    KOi K10771.
    OMAi IEKPSDH.
    OrthoDBi EOG7C8GJ6.
    PhylomeDBi P28352.
    TreeFami TF315048.

    Enzyme and pathway databases

    Reactomei REACT_219337. Removal of DNA patch containing abasic residue.
    REACT_219627. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.
    REACT_220827. Displacement of DNA glycosylase by APE1.
    REACT_227394. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.

    Miscellaneous databases

    NextBioi 279621.
    PROi P28352.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28352.
    Bgeei P28352.
    CleanExi MM_APEX1.
    Genevestigatori P28352.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR020848. AP_endonuclease_F1_CS.
    IPR005135. Endo/exonuclease/phosphatase.
    [Graphical view ]
    PANTHERi PTHR22748. PTHR22748. 1 hit.
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 1 hit.
    TIGRFAMsi TIGR00633. xth. 1 hit.
    PROSITEi PS00726. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III."
      Seki S., Akiyama K., Watanabe S., Hatsushika M., Ikeda S., Tsutsui K.
      J. Biol. Chem. 266:20797-20802(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NFS.
      Tissue: Spleen.
    2. "Genomic structure of the mouse apurinic/apyrimidinic endonuclease gene."
      Takiguchi Y., Chen D.J.
      Mamm. Genome 5:717-722(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
      Tissue: Embryo.
    3. "Cloning, sequence analysis, and chromosomal assignment of the mouse Apex gene."
      Akiyama K., Nagao K., Oshida T., Tsutsui K., Yoshida M.C., Seki S.
      Genomics 26:63-69(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
      Tissue: Blood.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    5. "A mouse DNA repair enzyme (APEX nuclease) having exonuclease and apurinic/apyrimidinic endonuclease activities: purification and characterization."
      Seki S., Ikeda S., Watanabe S., Hatsushika M., Tsutsui K., Akiyama K., Zhang B.
      Biochim. Biophys. Acta 1079:57-64(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22, CHARACTERIZATION.
      Tissue: Ascites.
    6. "Identification and characterization of mitochondrial abasic (AP)-endonuclease in mammalian cells."
      Chattopadhyay R., Wiederhold L., Szczesny B., Boldogh I., Hazra T.K., Izumi T., Mitra S.
      Nucleic Acids Res. 34:2067-2076(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "APE1- and APE2-dependent DNA breaks in immunoglobulin class switch recombination."
      Guikema J.E., Linehan E.K., Tsuchimoto D., Nakabeppu Y., Strauss P.R., Stavnezer J., Schrader C.E.
      J. Exp. Med. 204:3017-3026(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Apex2 is required for efficient somatic hypermutation but not for class switch recombination of immunoglobulin genes."
      Sabouri Z., Okazaki I.M., Shinkura R., Begum N., Nagaoka H., Tsuchimoto D., Nakabeppu Y., Honjo T.
      Int. Immunol. 21:947-955(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The role of Cdk5-mediated apurinic/apyrimidinic endonuclease 1 phosphorylation in neuronal death."
      Huang E., Qu D., Zhang Y., Venderova K., Haque M.E., Rousseaux M.W.C., Slack R.S., Woulfe J.M., Park D.S.
      Nat. Cell Biol. 12:563-571(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-232, INTERACTION WITH CDK5, MUTAGENESIS OF THR-232.

    Entry informationi

    Entry nameiAPEX1_MOUSE
    AccessioniPrimary (citable) accession number: P28352
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The specific activity of the cleaved mitochondrial endodeoxyribonuclease appeared to be about 3-fold higher than of the full-length form. Extract of mitochondria, but not of nuclei or cytosol, cleaves recombinant APEX1 to generate a mitochondrial APEX1-sized product By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3