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P28352

- APEX1_MOUSE

UniProt

P28352 - APEX1_MOUSE

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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

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. poly(A) RNA binding Source: Ensembl
  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
Complete GO annotation...

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-KW
  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
Complete GO annotation...

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

BgeeiP28352.
CleanExiMM_APEX1.
ExpressionAtlasiP28352. baseline and differential.
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

        10         20         30         40         50
MPKRGKKAAA DDGEEPKSEP ETKKSKGAAK KTEKEAAGEG PVLYEDPPDQ
60 70 80 90 100
KTSPSGKSAT LKICSWNVDG LRAWIKKKGL DWVKEEAPDI LCLQETKCSE
110 120 130 140 150
NKLPAELQEL PGLTHQYWSA PSDKEGYSGV GLLSRQCPLK VSYGIGEEEH
160 170 180 190 200
DQEGRVIVAE FESFVLVTAY VPNAGRGLVR LEYRQRWDEA FRKFLKDLAS
210 220 230 240 250
RKPLVLCGDL NVAHEEIDLR NPKGNKKNAG FTPQERQGFG ELLQAVPLAD
260 270 280 290 300
SFRHLYPNTA YAYTFWTYMM NARSKNVGWR LDYFLLSHSL LPALCDSKIR
310
SKALGSDHCP ITLYLAL
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

Bgeei P28352.
CleanExi MM_APEX1.
ExpressionAtlasi P28352. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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