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P27695 (APEX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Short name=APE-1
REF-1
Redox factor-1
Gene names
Name:APEX1
Synonyms:APE, APE1, APEX, APX, HAP1, REF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

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. Ref.1 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.32 Ref.35 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.45 Ref.46 Ref.48 Ref.49

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. Ref.21 Ref.30 Ref.39 Ref.49 Ref.52

Cofactor

Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit. Ref.21 Ref.39 Ref.49 Ref.52

Enzyme regulation

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

Subunit structure

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. Ref.14 Ref.17 Ref.19 Ref.20 Ref.26 Ref.28 Ref.29 Ref.31 Ref.36 Ref.40 Ref.42 Ref.44 Ref.45 Ref.46

Subcellular location

Nucleus. Nucleusnucleolus. Nucleus speckle. Endoplasmic reticulum. Cytoplasm. Note: Detected in the cytoplasm of B-cells stimulated to switch By similarity. 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 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. Ref.14 Ref.19 Ref.22 Ref.23 Ref.24 Ref.31 Ref.33 Ref.34 Ref.36 Ref.40 Ref.44 Ref.45

DNA-(apurinic or apyrimidinic site) lyase, mitochondrial: Mitochondrion. Note: The cleaved APEX2 is only detected in mitochondria By similarity. 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. Ref.14 Ref.19 Ref.22 Ref.23 Ref.24 Ref.31 Ref.33 Ref.34 Ref.36 Ref.40 Ref.44 Ref.45

Induction

Up-regulated in presence of reactive oxygen species (ROS), like bleomycin, H2O2 and phenazine methosulfate. Ref.22

Domain

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.

Post-translational modification

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. Phosphorylation of Thr-233 by CDK5 reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death. Ref.23 Ref.25

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. Ref.29 Ref.46

Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxynuclease 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.

Cys-65 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES).

Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation. Ref.42

Miscellaneous

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

Sequence similarities

Belongs to the DNA repair enzymes AP/ExoA family.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Transcription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
Magnesium
Metal-binding
RNA-binding
   Molecular functionActivator
Endonuclease
Exonuclease
Hydrolase
Lyase
Nuclease
Repressor
   PTMAcetylation
Cleavage on pair of basic residues
Disulfide bond
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay Ref.40. Source: GOC

DNA demethylation

Inferred from direct assay Ref.48. Source: UniProtKB

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from direct assay Ref.22. Source: UniProtKB

RNA phosphodiester bond hydrolysis, endonucleolytic

Traceable author statement Ref.52. Source: GOC

aging

Inferred from electronic annotation. Source: Ensembl

base-excision repair

Traceable author statement. Source: Reactome

cell redox homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay PubMed 11478795Ref.27. Source: GOC

oxidation-reduction process

Inferred from direct assay Ref.14PubMed 9119221. Source: GOC

positive regulation of DNA repair

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of mRNA stability

Inferred from mutant phenotype Ref.41. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to drug

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay Ref.22. Source: UniProtKB

endoplasmic reticulum

Traceable author statement Ref.14. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.44. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.33. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.33Ref.40. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.33. Source: UniProtKB

nucleus

Inferred from direct assay Ref.31Ref.45PubMed 9119221. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

ribosome

Traceable author statement Ref.14. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3'-5' exonuclease activity

Inferred from direct assay Ref.27. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.52. Source: UniProtKB

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from direct assay Ref.40. Source: UniProtKB

RNA-DNA hybrid ribonuclease activity

Traceable author statement Ref.52. Source: UniProtKB

chromatin DNA binding

Inferred from direct assay Ref.28. Source: UniProtKB

damaged DNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

endodeoxyribonuclease activity

Traceable author statement Ref.2. Source: ProtInc

endonuclease activity

Inferred from direct assay PubMed 11478795. Source: MGI

metal ion binding

Inferred from direct assay Ref.52. Source: UniProtKB

oxidoreductase activity

Inferred from direct assay Ref.14PubMed 9119221. Source: UniProtKB

phosphodiesterase I activity

Traceable author statement PubMed 9119221. Source: UniProtKB

phosphoric diester hydrolase activity

Inferred from direct assay PubMed 11478795. Source: MGI

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.24Ref.28Ref.14PubMed 15518571Ref.31Ref.36Ref.40PubMed 19465398PubMed 19505873Ref.45Ref.44Ref.17Ref.20. Source: UniProtKB

site-specific endodeoxyribonuclease activity, specific for altered base

Inferred from direct assay Ref.40. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 9119221. Source: UniProtKB

transcription corepressor activity

Traceable author statement PubMed 7961715. Source: ProtInc

uracil DNA N-glycosylase activity

Traceable author statement PubMed 10805771. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.14
Chain2 – 318317DNA-(apurinic or apyrimidinic site) lyase
PRO_0000200010
Chain32 – 318287DNA-(apurinic or apyrimidinic site) lyase, mitochondrial By similarity
PRO_0000402572

Regions

Region2 – 3332Necessary for interaction with YBX1, binding to RNA, NPM1-dependent association with rRNA, endoribonuclease activity on abasic RNA and localization in the nucleoli
Region8 – 136Nuclear localization signal (NLS)
Region23 – 3311Necessary for interaction with NPM1 and for efficient rRNA binding
Region64 – 8017Nuclear export signal (NES)
Region289 – 31830Mitochondrial targeting sequence (MTS)

Sites

Active site1711 Ref.30 Ref.49
Active site2101Proton donor/acceptor Ref.30 Ref.49
Metal binding701Magnesium 1
Metal binding961Magnesium 1
Metal binding2101Magnesium 2
Metal binding2121Magnesium 2
Metal binding3081Magnesium 1
Site31 – 322Cleavage; by granzyme A
Site2121Transition state stabilizer
Site2831Important for catalytic activity
Site3091Interaction with DNA substrate

Amino acid modifications

Modified residue61N6-acetyllysine; by EP300 Ref.29
Modified residue71N6-acetyllysine; by EP300 Ref.29
Modified residue271N6-acetyllysine Ref.46
Modified residue311N6-acetyllysine Ref.46
Modified residue321N6-acetyllysine Ref.46
Modified residue351N6-acetyllysine Ref.46
Modified residue651S-nitrosocysteine; alternate Ref.34
Modified residue931S-nitrosocysteine; alternate Ref.34
Modified residue1971N6-acetyllysine Ref.43
Modified residue2331Phosphothreonine; by CDK5 By similarity
Modified residue3101S-nitrosocysteine Ref.34
Disulfide bond65 ↔ 93Alternate Probable

Natural variations

Natural variant511Q → H. Ref.11
Corresponds to variant rs1048945 [ dbSNP | Ensembl ].
VAR_013455
Natural variant641I → V. Ref.11
Corresponds to variant rs2307486 [ dbSNP | Ensembl ].
VAR_014823
Natural variant1481D → E. Ref.11 Ref.13
Corresponds to variant rs1130409 [ dbSNP | Ensembl ].
VAR_019790

Experimental info

Mutagenesis61K → R: Lack of acetylation, does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-7. Does not inhibit interaction with HDAC1, HDAC2 and HDAC3. Absence of increase in nCaRE binding activity. Ref.29 Ref.31 Ref.36 Ref.45
Mutagenesis71K → R: Lack of acetylation and does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-6. Ref.29 Ref.31 Ref.36 Ref.45
Mutagenesis121E → A: Reduces nuclear localization; when associated with A-13. Ref.31
Mutagenesis131D → A: Reduces nuclear localization; when associated with A-12. Ref.31
Mutagenesis241K → A: Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-25; A-27; A-31 and A-32. Inhibits ubiquitination; when associated with K-25 and K-27. Ref.42 Ref.44 Ref.46
Mutagenesis251K → A: Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-27; A-31 and A-32. Inhibits ubiquitination; when associated with K-24 and K-27. Ref.42 Ref.44 Ref.46
Mutagenesis271K → A: Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoyribonuclease activity; when associated with A-24; A-25; A-31 and A-32. Inhibits ubiquitination; when associated with K-24 and K-25. Ref.42 Ref.44 Ref.46
Mutagenesis311K → A: Enhances the interaction with TOMM20. Does not inhibit redox and AP endodeoyribonuclease activities. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-32. Reduces protection from granzyme A-mediated cell death; when associated with A-65 and A-210. Ref.14 Ref.44 Ref.46
Mutagenesis321K → A: Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-31. Ref.46
Mutagenesis651C → A: Abolishes the redox activity. Does not abolish the AP endodeoxyribonuclease and phosphodiesterase activities. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-210. Ref.14 Ref.16 Ref.38
Mutagenesis651C → S: Does not abolish NO-induced nitrosylation. Enhances NO-induced nuclear export. Ref.14 Ref.16 Ref.38
Mutagenesis681N → A: Nearly abolishes AP endodeoxyribonuclease activity. Ref.49
Mutagenesis701D → A: Strongly reduces AP endodeoxyribonuclease activity. Ref.49
Mutagenesis931C → A: Abolishes partially the redox activity. Ref.16 Ref.38
Mutagenesis931C → S: Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-310. Ref.16 Ref.38
Mutagenesis961E → A: Lacks MYC CRD RNA cleavage activity. Ref.41
Mutagenesis991C → A: Does not abolish the redox activity. Ref.16 Ref.38
Mutagenesis1381C → A: Does not abolish the redox activity. Ref.16 Ref.38
Mutagenesis1711Y → A, F or H: Abolishes the AP endodeoxyribonuclease activity. Ref.30 Ref.49
Mutagenesis2081C → A: Does not abolish the redox activity. Ref.16 Ref.38
Mutagenesis2101D → A or N: Abolishes the AP endodeoxyribonuclease activity. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-65. Ref.14
Mutagenesis2121N → A: Abolishes AP endodeoxyribonuclease activity. Ref.18
Mutagenesis2121N → Q or D: Decreases AP endodeoxyribonuclease activity. Ref.18
Mutagenesis2661F → A: Strongly reduces AP endodeoxyribonuclease activity. Ref.49
Mutagenesis2831D → A: Strongly reduces AP endodeoxyribonuclease activity, but does not affect RNA cleavage activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-308. Ref.21 Ref.49
Mutagenesis2961C → A: Does not abolish the redox activity. Ref.16 Ref.38
Mutagenesis2991K → A: Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-301. Ref.44
Mutagenesis3011R → A: Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-299. Ref.44
Mutagenesis3031K → A: Reduces the interaction with TOMM20. Ref.44
Mutagenesis3081D → A: Reduces AP endodeoxyribonuclease activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-283. Ref.21 Ref.49
Mutagenesis3091H → N or S: Abolishes AP endodeoxyribonuclease activity. Lacks MYC CRD RNA cleavage activity. Ref.21 Ref.41 Ref.49
Mutagenesis3101C → A: Does not abolish the redox activity. Ref.16 Ref.38
Mutagenesis3101C → S: Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-93. Ref.16 Ref.38
Sequence conflict571G → A in AAA58371. Ref.2
Sequence conflict3061G → A in AAA58371. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P27695 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B88579C01BAF80C6

FASTA31835,555
        10         20         30         40         50         60 
MPKRGKKGAV AEDGDELRTE PEAKKSKTAA KKNDKEAAGE GPALYEDPPD QKTSPSGKPA 

        70         80         90        100        110        120 
TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS ENKLPAELQE LPGLSHQYWS 

       130        140        150        160        170        180 
APSDKEGYSG VGLLSRQCPL KVSYGIGDEE HDQEGRVIVA EFDSFVLVTA YVPNAGRGLV 

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

       250        260        270        280        290        300 
GELLQAVPLA DSFRHLYPNT PYAYTFWTYM MNARSKNVGW RLDYFLLSHS LLPALCDSKI 

       310 
RSKALGSDHC PITLYLAL 

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References

« Hide 'large scale' references
[1]"Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants."
Robson C.N., Hickson I.D.
Nucleic Acids Res. 19:5519-5523(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Melanocyte.
[2]"Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes."
Demple B., Herman T., Chen D.S.
Proc. Natl. Acad. Sci. U.S.A. 88:11450-11454(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III."
Seki S., Hatsushika M., Watanabe S., Akiyama K., Nagao K., Tsutsui K.
Biochim. Biophys. Acta 1131:287-299(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Bone marrow and Leukocyte.
[4]"Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme."
Xanthoudakis S., Miao G., Wang F., Pan Y.-C.E., Curran T.
EMBO J. 11:3323-3335(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21.
[5]"Nucleotide sequence of a cDNA for an apurinic/apyrimidinic endonuclease from HeLa cells."
Cheng X.B., Bunville J., Patterson T.A.
Nucleic Acids Res. 20:370-370(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Carcinoma.
[6]"The human gene for apurinic/apyrimidinic endonuclease (HAP1): sequence and localization to chromosome 14 band q12."
Zhao B., Grandy D.K., Hagerup J.M., Magenis R.E., Smith L., Chauhan B.C., Henner W.D.
Nucleic Acids Res. 20:4097-4098(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leukocyte.
[7]"Structure of the human DNA repair gene HAP1 and its localisation to chromosome 14q 11.2-12."
Robson C.N., Hocchauser D., Craig R., Rack K., Buckle I.D., Hickson I.D.
Nucleic Acids Res. 20:4417-4421(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Structure, promoter analysis and chromosomal assignment of the human APEX gene."
Akiyama K., Seki S., Oshida T., Yoshida M.
Biochim. Biophys. Acta 1219:15-25(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[10]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]NIEHS SNPs program
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-51; VAL-64 AND GLU-148.
[12]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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], VARIANT GLU-148.
Tissue: Brain, Lung and Skin.
[14]"Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, FUNCTION, INTERACTION WITH GZMA, CLEAVAGE BY GRANZYME A, IDENTIFICATION IN THE SET COMPLEX, MUTAGENESIS OF LYS-31; CYS-65 AND ASP-210, SUBCELLULAR LOCATION.
[15]"Human apurinic endonuclease gene (APE): structure and genomic mapping (chromosome 14q11.2-12)."
Harrison L., Ascione G., Menninger J.C., Ward D.C., Demple B.
Hum. Mol. Genet. 1:677-680(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
Tissue: Placenta.
[16]"Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding."
Walker L.J., Robson C.N., Black E., Gillespie D., Hickson I.D.
Mol. Cell. Biol. 13:5370-5376(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-65; CYS-93; CYS-99; CYS-138; CYS-208; CYS-296 AND CYS-310.
[17]"The interaction between Ku antigen and REF1 protein mediates negative gene regulation by extracellular calcium."
Chung U., Igarashi T., Nishishita T., Iwanari H., Iwamatsu A., Suwa A., Mimori T., Hata K., Ebisu S., Ogata E., Fujita T., Okazaki T.
J. Biol. Chem. 271:8593-8598(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH XRCC5 AND XRCC6.
[18]"Asparagine 212 is essential for abasic site recognition by the human DNA repair endonuclease HAP1."
Rothwell D.G., Hickson I.D.
Nucleic Acids Res. 24:4217-4221(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASN-212.
[19]"AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1."
Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J.
Proc. Natl. Acad. Sci. U.S.A. 94:3633-3638(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH TXN, SUBCELLULAR LOCATION.
[20]"Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway."
Bennett R.A., Wilson D.M. III, Wong D., Demple B.
Proc. Natl. Acad. Sci. U.S.A. 94:7166-7169(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POLB.
[21]"Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium."
Masuda Y., Bennett R.A., Demple B.
J. Biol. Chem. 273:30360-30365(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-283; ASP-308 AND HIS-309, COFACTOR.
[22]"Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals."
Ramana C.V., Boldogh I., Izumi T., Mitra S.
Proc. Natl. Acad. Sci. U.S.A. 95:5061-5066(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
[23]"Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1."
Fritz G., Kaina B.
Oncogene 18:1033-1040(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY CKII, SUBCELLULAR LOCATION.
[24]"Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation."
Wei S.J., Botero A., Hirota K., Bradbury C.M., Markovina S., Laszlo A., Spitz D.R., Goswami P.C., Yodoi J., Gius D.
Cancer Res. 60:6688-6695(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[25]"Activation of APE/Ref-1 redox activity is mediated by reactive oxygen species and PKC phosphorylation."
Hsieh M.M., Hegde V., Kelley M.R., Deutsch W.A.
Nucleic Acids Res. 29:3116-3122(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY PKC.
[26]"HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A."
Fan Z., Beresford P.J., Zhang D., Lieberman J.
Mol. Cell. Biol. 22:2810-2820(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET COMPLEX.
[27]"An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3' mispaired DNA."
Chou K.M., Cheng Y.C.
Nature 415:655-659(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter."
Kuninger D.T., Izumi T., Papaconstantinou J., Mitra S.
Nucleic Acids Res. 30:823-829(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HNRNPL.
[29]"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene."
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.
EMBO J. 22:6299-6309(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1; HDAC2 AND HDAC3, ACETYLATION AT LYS-6 AND LYS-7, MUTAGENESIS OF LYS-6 AND LYS-7.
[30]"Novel role of tyrosine in catalysis by human AP endonuclease 1."
Mundle S.T., Fattal M.H., Melo L.F., Coriolan J.D., O'Regan N.E., Strauss P.R.
DNA Repair 3:1447-1455(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF TYR-171.
[31]"Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1)."
Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.
Nucleic Acids Res. 33:3303-3312(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNA1 AND KPNA2, MUTAGENESIS OF LYS-6; LYS-7; GLU-12 AND ASP-13, SUBCELLULAR LOCATION.
[32]"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: FUNCTION.
[33]"UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles."
Campalans A., Amouroux R., Bravard A., Epe B., Radicella J.P.
J. Cell Sci. 120:23-32(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[34]"Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310."
Qu J., Liu G.H., Huang B., Chen C.
Nucleic Acids Res. 35:2522-2532(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-65; CYS-93 AND CYS-310 IN RESPONSE TO NITRIC OXIDE, SUBCELLULAR LOCATION.
[35]"Characterization of abasic endonuclease activity of human Ape1 on alternative substrates, as well as effects of ATP and sequence context on AP site incision."
Berquist B.R., McNeill D.R., Wilson D.M. III
J. Mol. Biol. 379:17-27(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[36]"Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1."
Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K., Kohno K., Mitra S., Bhakat K.K.
Mol. Cell. Biol. 28:7066-7080(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MVP AND YBX1, MUTAGENESIS OF LYS-6 AND LYS-7, SUBCELLULAR LOCATION.
[37]"Granzyme K degrades the redox/DNA repair enzyme Ape1 to trigger oxidative stress of target cells leading to cytotoxicity."
Guo Y., Chen J., Zhao T., Fan Z.
Mol. Immunol. 45:2225-2235(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[38]"Evolution of the redox function in mammalian apurinic/apyrimidinic endonuclease."
Georgiadis M.M., Luo M., Gaur R.K., Delaplane S., Li X., Kelley M.R.
Mutat. Res. 643:54-63(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-65; CYS-93; CYS-99; CYS-138; CYS-208; CYS-296 AND CYS-310.
[39]"Enzymatic mechanism of human apurinic/apyrimidinic endonuclease against a THF AP site model substrate."
Mundle S.T., Delaney J.C., Essigmann J.M., Strauss P.R.
Biochemistry 48:19-26(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME MECHANISM.
[40]"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KRT8; NPM1; PRDX6; PRPF19; RPLP0 AND WDR77, RNA-BINDING, SUBCELLULAR LOCATION.
[41]"Identification of apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA."
Barnes T., Kim W.C., Mantha A.K., Kim S.E., Izumi T., Mitra S., Lee C.H.
Nucleic Acids Res. 37:3946-3958(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, MUTAGENESIS OF GLU-96 AND HIS-309.
[42]"Ubiquitination of mammalian AP endonuclease (APE1) regulated by the p53-MDM2 signaling pathway."
Busso C.S., Iwakuma T., Izumi T.
Oncogene 28:1616-1625(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDM2, UBIQUITINATION, MUTAGENESIS OF LYS-24; LYS-25 AND LYS-27.
[43]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"Identification and characterization of mitochondrial targeting sequence of human apurinic/apyrimidinic endonuclease 1."
Li M., Zhong Z., Zhu J., Xiang D., Dai N., Cao X., Qing Y., Yang Z., Xie J., Li Z., Baugh L., Wang G., Wang D.
J. Biol. Chem. 285:14871-14881(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOMM20, MUTAGENESIS OF LYS-24; LYS-25; LYS-27; LYS-31; LYS-299; ARG-301 AND LYS-303, SUBCELLULAR LOCATION.
[45]"SIRT1 deacetylates APE1 and regulates cellular base excision repair."
Yamamori T., DeRicco J., Naqvi A., Hoffman T.A., Mattagajasingh I., Kasuno K., Jung S.B., Kim C.S., Irani K.
Nucleic Acids Res. 38:832-845(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIRT1 AND XRCC1, MUTAGENESIS OF LYS-6 AND LYS-7, SUBCELLULAR LOCATION.
[46]"Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions."
Fantini D., Vascotto C., Marasco D., D'Ambrosio C., Romanello M., Vitagliano L., Pedone C., Poletto M., Cesaratto L., Quadrifoglio F., Scaloni A., Radicella J.P., Tell G.
Nucleic Acids Res. 38:8239-8256(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NPM1, RNA-BINDING, ACETYLATION AT LYS-27; LYS-31; LYS-32 AND LYS-35, MUTAGENESIS OF LYS-24; LYS-25; LYS-27; LYS-31 AND LYS-32, IDENTIFICATION BY MASS SPECTROMETRY.
[47]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[48]"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain."
Guo J.U., Su Y., Zhong C., Ming G.L., Song H.
Cell 145:423-434(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DEMETHYLATION.
[49]"Characterization of the endoribonuclease active site of human apurinic/apyrimidinic endonuclease 1."
Kim W.C., Berquist B.R., Chohan M., Uy C., Wilson D.M. III, Lee C.H.
J. Mol. Biol. 411:960-971(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-68; ASP-70; TYR-171; PHE-266; ASP-283; ASP-308 AND HIS-309, CATALYTIC ACTIVITY, ACTIVE SITE, FUNCTION, COFACTOR.
[50]"The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites."
Gorman M.A., Morera S., Rothwell D.G., de La Fortelle E., Mol C.D., Tainer J.A., Hickson I.D., Freemont P.S.
EMBO J. 16:6548-6558(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 32-318 IN COMPLEX WITH METAL IONS.
[51]"DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination."
Mol C.D., Izumi T., Mitra S., Tainer J.A.
Nature 403:451-456(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 40-318 IN COMPLEX WITH DNA AND METAL ION, DNA-BINDING.
[52]"Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism."
Beernink P.T., Segelke B.W., Hadi M.Z., Erzberger J.P., Wilson D.M. III, Rupp B.
J. Mol. Biol. 307:1023-1034(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH METAL IONS, CATALYTIC ACTIVITY, COFACTOR.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59764 mRNA. Translation: CAA42437.1.
M80261 mRNA. Translation: AAA58371.1.
D90373 mRNA. Translation: BAA14381.1.
S43127 mRNA. Translation: AAB22977.1.
M81955 mRNA. Translation: AAA58372.1.
M92444 Genomic DNA. Translation: AAA58629.1.
X66133 Genomic DNA. Translation: CAA46925.1.
D13370 Genomic DNA. Translation: BAA02633.1.
U79268 mRNA. Translation: AAB50212.1.
BT007236 mRNA. Translation: AAP35900.1.
AF488551 Genomic DNA. Translation: AAL86909.1.
AL355075 Genomic DNA. No translation available.
BC002338 mRNA. Translation: AAH02338.1.
BC004979 mRNA. Translation: AAH04979.1.
BC008145 mRNA. Translation: AAH08145.1.
BC019291 mRNA. Translation: AAH19291.1.
M99703 Genomic DNA. Translation: AAA58373.1.
CCDSCCDS9550.1.
PIRS23550.
RefSeqNP_001231178.1. NM_001244249.1.
NP_001632.2. NM_001641.3.
NP_542379.1. NM_080648.2.
NP_542380.1. NM_080649.2.
XP_005267638.1. XM_005267581.2.
UniGeneHs.73722.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BIXX-ray2.20A32-318[»]
1CQGNMR-B59-71[»]
1CQHNMR-B59-71[»]
1DE8X-ray2.95A/B43-318[»]
1DE9X-ray3.00A/B43-318[»]
1DEWX-ray2.65A/B40-318[»]
1E9NX-ray2.20A/B2-318[»]
1HD7X-ray1.95A2-318[»]
2ISIX-ray2.76A/B/C2-318[»]
2O3HX-ray1.90A40-318[»]
3U8UX-ray2.15A/B/C/D/E/F1-318[»]
4IEMX-ray2.39A/B/C/D2-318[»]
4LNDX-ray1.92A/B/C39-318[»]
DisProtDP00007.
ProteinModelPortalP27695.
SMRP27695. Positions 44-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106825. 66 interactions.
DIPDIP-6130N.
IntActP27695. 29 interactions.
MINTMINT-119189.
STRING9606.ENSP00000216714.

Chemistry

BindingDBP27695.
ChEMBLCHEMBL5619.
DrugBankDB04967. Lucanthone.

PTM databases

PhosphoSiteP27695.

Polymorphism databases

DMDM113984.

Proteomic databases

MaxQBP27695.
PaxDbP27695.
PeptideAtlasP27695.
PRIDEP27695.

Protocols and materials databases

DNASU328.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216714; ENSP00000216714; ENSG00000100823.
ENST00000398030; ENSP00000381111; ENSG00000100823.
ENST00000555414; ENSP00000451979; ENSG00000100823.
ENST00000557344; ENSP00000452137; ENSG00000100823.
GeneID328.
KEGGhsa:328.
UCSCuc001vxg.3. human.

Organism-specific databases

CTD328.
GeneCardsGC14P020924.
HGNCHGNC:587. APEX1.
HPACAB004294.
CAB047307.
HPA000956.
HPA002564.
MIM107748. gene.
neXtProtNX_P27695.
PharmGKBPA201059.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0708.
HOGENOMHOG000034586.
HOVERGENHBG050531.
InParanoidP27695.
KOK10771.
OMATCTSCEV.
OrthoDBEOG7C8GJ6.
PhylomeDBP27695.
TreeFamTF315048.

Enzyme and pathway databases

BRENDA4.2.99.18. 2681.
ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP27695.
BgeeP27695.
CleanExHS_APEX1.
HS_HAP1.
GenevestigatorP27695.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR004808. AP_endonuc_1.
IPR020847. AP_endonuclease_F1_BS.
IPR020848. AP_endonuclease_F1_CS.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERPTHR22748. PTHR22748. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
TIGRFAMsTIGR00633. 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...

Other

ChiTaRSAPEX1. human.
EvolutionaryTraceP27695.
GeneWikiAPEX1.
GenomeRNAi328.
NextBio1347.
PMAP-CutDBP27695.
PROP27695.
SOURCESearch...

Entry information

Entry nameAPEX1_HUMAN
AccessionPrimary (citable) accession number: P27695
Secondary accession number(s): Q969L5, Q99775
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 183 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 14

Human chromosome 14: entries, gene names and cross-references to MIM