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DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]

 APEX1_HUMAN             Reviewed;         318 AA.
P27695; Q969L5; Q99775;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 217.
RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
EC=3.1.-.-;
EC=4.2.99.18;
AltName: Full=APEX nuclease;
Short=APEN;
AltName: Full=Apurinic-apyrimidinic endonuclease 1;
Short=AP endonuclease 1;
Short=APE-1;
AltName: Full=REF-1;
AltName: Full=Redox factor-1;
Contains:
RecName: Full=DNA-(apurinic or apyrimidinic site) lyase, mitochondrial;
Name=APEX1; Synonyms=APE, APE1, APEX, APX, HAP1, REF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Melanocyte;
PubMed=1719477; DOI=10.1093/nar/19.20.5519;
Robson C.N., Hickson I.D.;
"Isolation of cDNA clones encoding a human apurinic/apyrimidinic
endonuclease that corrects DNA repair and mutagenesis defects in E.
coli xth (exonuclease III) mutants.";
Nucleic Acids Res. 19:5519-5523(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1722334; DOI=10.1073/pnas.88.24.11450;
Demple B., Herman T., Chen D.S.;
"Cloning and expression of APE, the cDNA encoding the major human
apurinic endonuclease: definition of a family of DNA repair enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 88:11450-11454(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Bone marrow, and Leukocyte;
PubMed=1627644; DOI=10.1016/0167-4781(92)90027-W;
Seki S., Hatsushika M., Watanabe S., Akiyama K., Nagao K., Tsutsui K.;
"cDNA cloning, sequencing, expression and possible domain structure of
human APEX nuclease homologous to Escherichia coli exonuclease III.";
Biochim. Biophys. Acta 1131:287-299(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-21.
PubMed=1380454;
Xanthoudakis S., Miao G., Wang F., Pan Y.-C.E., Curran T.;
"Redox activation of Fos-Jun DNA binding activity is mediated by a DNA
repair enzyme.";
EMBO J. 11:3323-3335(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Carcinoma;
PubMed=1371347; DOI=10.1093/nar/20.2.370;
Cheng X.B., Bunville J., Patterson T.A.;
"Nucleotide sequence of a cDNA for an apurinic/apyrimidinic
endonuclease from HeLa cells.";
Nucleic Acids Res. 20:370-370(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=1380694; DOI=10.1093/nar/20.15.4097;
Zhao B., Grandy D.K., Hagerup J.M., Magenis R.E., Smith L.,
Chauhan B.C., Henner W.D.;
"The human gene for apurinic/apyrimidinic endonuclease (HAP1):
sequence and localization to chromosome 14 band q12.";
Nucleic Acids Res. 20:4097-4098(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1383925; DOI=10.1093/nar/20.17.4417;
Robson C.N., Hocchauser D., Craig R., Rack K., Buckle I.D.,
Hickson I.D.;
"Structure of the human DNA repair gene HAP1 and its localisation to
chromosome 14q 11.2-12.";
Nucleic Acids Res. 20:4417-4421(1992).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8086453; DOI=10.1016/0167-4781(94)90241-0;
Akiyama K., Seki S., Oshida T., Yoshida M.;
"Structure, promoter analysis and chromosomal assignment of the human
APEX gene.";
Biochim. Biophys. Acta 1219:15-25(1994).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9110174;
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.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-51; VAL-64 AND
GLU-148.
NIEHS SNPs program;
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
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., 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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-148.
TISSUE=Brain, Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
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, AND SUBCELLULAR LOCATION.
PubMed=12524539; DOI=10.1038/ni885;
Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A.,
Pommier Y., Lieberman J.;
"Cleaving the oxidative repair protein Ape1 enhances cell death
mediated by granzyme A.";
Nat. Immunol. 4:145-153(2003).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
TISSUE=Placenta;
PubMed=1284593; DOI=10.1093/hmg/1.9.677;
Harrison L., Ascione G., Menninger J.C., Ward D.C., Demple B.;
"Human apurinic endonuclease gene (APE): structure and genomic mapping
(chromosome 14q11.2-12).";
Hum. Mol. Genet. 1:677-680(1992).
[16]
FUNCTION, AND MUTAGENESIS OF CYS-65; CYS-93; CYS-99; CYS-138; CYS-208;
CYS-296 AND CYS-310.
PubMed=8355688; DOI=10.1128/MCB.13.9.5370;
Walker L.J., Robson C.N., Black E., Gillespie D., Hickson I.D.;
"Identification of residues in the human DNA repair enzyme HAP1 (Ref-
1) that are essential for redox regulation of Jun DNA binding.";
Mol. Cell. Biol. 13:5370-5376(1993).
[17]
FUNCTION, AND INTERACTION WITH XRCC5 AND XRCC6.
PubMed=8621488; DOI=10.1074/jbc.271.15.8593;
Chung U., Igarashi T., Nishishita T., Iwanari H., Iwamatsu A.,
Suwa A., Mimori T., Hata K., Ebisu S., Ogata E., Fujita T.,
Okazaki T.;
"The interaction between Ku antigen and REF1 protein mediates negative
gene regulation by extracellular calcium.";
J. Biol. Chem. 271:8593-8598(1996).
[18]
FUNCTION, AND MUTAGENESIS OF ASN-212.
PubMed=8932375; DOI=10.1093/nar/24.21.4217;
Rothwell D.G., Hickson I.D.;
"Asparagine 212 is essential for abasic site recognition by the human
DNA repair endonuclease HAP1.";
Nucleic Acids Res. 24:4217-4221(1996).
[19]
FUNCTION, SUBUNIT, INTERACTION WITH TXN, AND SUBCELLULAR LOCATION.
PubMed=9108029; DOI=10.1073/pnas.94.8.3633;
Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J.;
"AP-1 transcriptional activity is regulated by a direct association
between thioredoxin and Ref-1.";
Proc. Natl. Acad. Sci. U.S.A. 94:3633-3638(1997).
[20]
FUNCTION, AND INTERACTION WITH POLB.
PubMed=9207062; DOI=10.1073/pnas.94.14.7166;
Bennett R.A., Wilson D.M. III, Wong D., Demple B.;
"Interaction of human apurinic endonuclease and DNA polymerase beta in
the base excision repair pathway.";
Proc. Natl. Acad. Sci. U.S.A. 94:7166-7169(1997).
[21]
CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-283; ASP-308 AND
HIS-309, AND COFACTOR.
PubMed=9804799; DOI=10.1074/jbc.273.46.30360;
Masuda Y., Bennett R.A., Demple B.;
"Rapid dissociation of human apurinic endonuclease (Ape1) from incised
DNA induced by magnesium.";
J. Biol. Chem. 273:30360-30365(1998).
[22]
FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=9560228; DOI=10.1073/pnas.95.9.5061;
Ramana C.V., Boldogh I., Izumi T., Mitra S.;
"Activation of apurinic/apyrimidinic endonuclease in human cells by
reactive oxygen species and its correlation with their adaptive
response to genotoxicity of free radicals.";
Proc. Natl. Acad. Sci. U.S.A. 95:5061-5066(1998).
[23]
FUNCTION, PHOSPHORYLATION BY CKII, AND SUBCELLULAR LOCATION.
PubMed=10023679; DOI=10.1038/sj.onc.1202394;
Fritz G., Kaina B.;
"Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects
redox regulation of AP-1.";
Oncogene 18:1033-1040(1999).
[24]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11118054;
Wei S.J., Botero A., Hirota K., Bradbury C.M., Markovina S.,
Laszlo A., Spitz D.R., Goswami P.C., Yodoi J., Gius D.;
"Thioredoxin nuclear translocation and interaction with redox factor-1
activates the activator protein-1 transcription factor in response to
ionizing radiation.";
Cancer Res. 60:6688-6695(2000).
[25]
FUNCTION, AND PHOSPHORYLATION BY PKC.
PubMed=11452037; DOI=10.1093/nar/29.14.3116;
Hsieh M.M., Hegde V., Kelley M.R., Deutsch W.A.;
"Activation of APE/Ref-1 redox activity is mediated by reactive oxygen
species and PKC phosphorylation.";
Nucleic Acids Res. 29:3116-3122(2001).
[26]
IDENTIFICATION IN THE SET COMPLEX.
PubMed=11909973; DOI=10.1128/MCB.22.8.2810-2820.2002;
Fan Z., Beresford P.J., Zhang D., Lieberman J.;
"HMG2 interacts with the nucleosome assembly protein SET and is a
target of the cytotoxic T-lymphocyte protease granzyme A.";
Mol. Cell. Biol. 22:2810-2820(2002).
[27]
FUNCTION.
PubMed=11832948; DOI=10.1038/415655a;
Chou K.M., Cheng Y.C.;
"An exonucleolytic activity of human apurinic/apyrimidinic
endonuclease on 3' mispaired DNA.";
Nature 415:655-659(2002).
[28]
FUNCTION, AND INTERACTION WITH HNRNPL.
PubMed=11809897; DOI=10.1093/nar/30.3.823;
Kuninger D.T., Izumi T., Papaconstantinou J., Mitra S.;
"Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like
repressor element in the AP-endonuclease 1 promoter.";
Nucleic Acids Res. 30:823-829(2002).
[29]
INTERACTION WITH HDAC1; HDAC2 AND HDAC3, ACETYLATION AT LYS-6 AND
LYS-7, AND MUTAGENESIS OF LYS-6 AND LYS-7.
PubMed=14633989; DOI=10.1093/emboj/cdg595;
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.;
"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation
of the parathyroid hormone gene.";
EMBO J. 22:6299-6309(2003).
[30]
CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF TYR-171.
PubMed=15380100; DOI=10.1016/j.dnarep.2004.06.009;
Mundle S.T., Fattal M.H., Melo L.F., Coriolan J.D., O'Regan N.E.,
Strauss P.R.;
"Novel role of tyrosine in catalysis by human AP endonuclease 1.";
DNA Repair 3:1447-1455(2004).
[31]
INTERACTION WITH KPNA1 AND KPNA2, MUTAGENESIS OF LYS-6; LYS-7; GLU-12
AND ASP-13, AND SUBCELLULAR LOCATION.
PubMed=15942031; DOI=10.1093/nar/gki641;
Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.;
"Analysis of nuclear transport signals in the human
apurinic/apyrimidinic endonuclease (APE1/Ref1).";
Nucleic Acids Res. 33:3303-3312(2005).
[32]
FUNCTION.
PubMed=16617147; DOI=10.1093/nar/gkl177;
Chattopadhyay R., Wiederhold L., Szczesny B., Boldogh I., Hazra T.K.,
Izumi T., Mitra S.;
"Identification and characterization of mitochondrial abasic (AP)-
endonuclease in mammalian cells.";
Nucleic Acids Res. 34:2067-2076(2006).
[33]
SUBCELLULAR LOCATION.
PubMed=17148573; DOI=10.1242/jcs.03312;
Campalans A., Amouroux R., Bravard A., Epe B., Radicella J.P.;
"UVA irradiation induces relocalisation of the DNA repair protein
hOGG1 to nuclear speckles.";
J. Cell Sci. 120:23-32(2007).
[34]
S-NITROSYLATION AT CYS-65; CYS-93 AND CYS-310 IN RESPONSE TO NITRIC
OXIDE, AND SUBCELLULAR LOCATION.
PubMed=17403694; DOI=10.1093/nar/gkl1163;
Qu J., Liu G.H., Huang B., Chen C.;
"Nitric oxide controls nuclear export of APE1/Ref-1 through S-
nitrosation of cysteines 93 and 310.";
Nucleic Acids Res. 35:2522-2532(2007).
[35]
FUNCTION.
PubMed=18439621; DOI=10.1016/j.jmb.2008.03.053;
Berquist B.R., McNeill D.R., Wilson D.M. III;
"Characterization of abasic endonuclease activity of human Ape1 on
alternative substrates, as well as effects of ATP and sequence context
on AP site incision.";
J. Mol. Biol. 379:17-27(2008).
[36]
FUNCTION, INTERACTION WITH MVP AND YBX1, MUTAGENESIS OF LYS-6 AND
LYS-7, AND SUBCELLULAR LOCATION.
PubMed=18809583; DOI=10.1128/MCB.00244-08;
Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K.,
Kohno K., Mitra S., Bhakat K.K.;
"Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-
mediated activation of the multidrug resistance gene MDR1.";
Mol. Cell. Biol. 28:7066-7080(2008).
[37]
FUNCTION.
PubMed=18179823; DOI=10.1016/j.molimm.2007.11.020;
Guo Y., Chen J., Zhao T., Fan Z.;
"Granzyme K degrades the redox/DNA repair enzyme Ape1 to trigger
oxidative stress of target cells leading to cytotoxicity.";
Mol. Immunol. 45:2225-2235(2008).
[38]
FUNCTION, AND MUTAGENESIS OF CYS-65; CYS-93; CYS-99; CYS-138; CYS-208;
CYS-296 AND CYS-310.
PubMed=18579163; DOI=10.1016/j.mrfmmm.2008.04.008;
Georgiadis M.M., Luo M., Gaur R.K., Delaplane S., Li X., Kelley M.R.;
"Evolution of the redox function in mammalian apurinic/apyrimidinic
endonuclease.";
Mutat. Res. 643:54-63(2008).
[39]
CATALYTIC ACTIVITY, COFACTOR, AND ENZYME MECHANISM.
PubMed=19123919; DOI=10.1021/bi8016137;
Mundle S.T., Delaney J.C., Essigmann J.M., Strauss P.R.;
"Enzymatic mechanism of human apurinic/apyrimidinic endonuclease
against a THF AP site model substrate.";
Biochemistry 48:19-26(2009).
[40]
FUNCTION, INTERACTION WITH KRT8; NPM1; PRDX6; PRPF19; RPLP0 AND WDR77,
RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
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.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[41]
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF GLU-96 AND HIS-309.
PubMed=19401441; DOI=10.1093/nar/gkp275;
Barnes T., Kim W.C., Mantha A.K., Kim S.E., Izumi T., Mitra S.,
Lee C.H.;
"Identification of apurinic/apyrimidinic endonuclease 1 (APE1) as the
endoribonuclease that cleaves c-myc mRNA.";
Nucleic Acids Res. 37:3946-3958(2009).
[42]
INTERACTION WITH MDM2, UBIQUITINATION, AND MUTAGENESIS OF LYS-24;
LYS-25 AND LYS-27.
PubMed=19219073; DOI=10.1038/onc.2009.5;
Busso C.S., Iwakuma T., Izumi T.;
"Ubiquitination of mammalian AP endonuclease (APE1) regulated by the
p53-MDM2 signaling pathway.";
Oncogene 28:1616-1625(2009).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[44]
INTERACTION WITH TOMM20, MUTAGENESIS OF LYS-24; LYS-25; LYS-27;
LYS-31; LYS-299; ARG-301 AND LYS-303, AND SUBCELLULAR LOCATION.
PubMed=20231292; DOI=10.1074/jbc.M109.069591;
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.;
"Identification and characterization of mitochondrial targeting
sequence of human apurinic/apyrimidinic endonuclease 1.";
J. Biol. Chem. 285:14871-14881(2010).
[45]
FUNCTION, INTERACTION WITH SIRT1 AND XRCC1, MUTAGENESIS OF LYS-6 AND
LYS-7, AND SUBCELLULAR LOCATION.
PubMed=19934257; DOI=10.1093/nar/gkp1039;
Yamamori T., DeRicco J., Naqvi A., Hoffman T.A., Mattagajasingh I.,
Kasuno K., Jung S.B., Kim C.S., Irani K.;
"SIRT1 deacetylates APE1 and regulates cellular base excision
repair.";
Nucleic Acids Res. 38:832-845(2010).
[46]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20699270; DOI=10.1093/nar/gkq691;
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.;
"Critical lysine residues within the overlooked N-terminal domain of
human APE1 regulate its biological functions.";
Nucleic Acids Res. 38:8239-8256(2010).
[47]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[48]
FUNCTION IN DNA DEMETHYLATION.
PubMed=21496894; DOI=10.1016/j.cell.2011.03.022;
Guo J.U., Su Y., Zhong C., Ming G.L., Song H.;
"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA
demethylation in the adult brain.";
Cell 145:423-434(2011).
[49]
MUTAGENESIS OF ASN-68; ASP-70; TYR-171; PHE-266; ASP-283; ASP-308 AND
HIS-309, CATALYTIC ACTIVITY, ACTIVE SITE, FUNCTION, AND COFACTOR.
PubMed=21762700; DOI=10.1016/j.jmb.2011.06.050;
Kim W.C., Berquist B.R., Chohan M., Uy C., Wilson D.M. III, Lee C.H.;
"Characterization of the endoribonuclease active site of human
apurinic/apyrimidinic endonuclease 1.";
J. Mol. Biol. 411:960-971(2011).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[53]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 32-318 IN COMPLEX WITH METAL
IONS.
PubMed=9351835; DOI=10.1093/emboj/16.21.6548;
Gorman M.A., Morera S., Rothwell D.G., de La Fortelle E., Mol C.D.,
Tainer J.A., Hickson I.D., Freemont P.S.;
"The crystal structure of the human DNA repair endonuclease HAP1
suggests the recognition of extra-helical deoxyribose at DNA abasic
sites.";
EMBO J. 16:6548-6558(1997).
[54]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 40-318 IN COMPLEX WITH DNA
AND METAL ION, AND DNA-BINDING.
PubMed=10667800; DOI=10.1038/35000249;
Mol C.D., Izumi T., Mitra S., Tainer J.A.;
"DNA-bound structures and mutants reveal abasic DNA binding by APE1
and DNA repair coordination.";
Nature 403:451-456(2000).
[55]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH METAL IONS,
CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=11286553; DOI=10.1006/jmbi.2001.4529;
Beernink P.T., Segelke B.W., Hadi M.Z., Erzberger J.P.,
Wilson D.M. III, Rupp B.;
"Two divalent metal ions in the active site of a new crystal form of
human apurinic/apyrimidinic endonuclease, Ape1: implications for the
catalytic mechanism.";
J. Mol. Biol. 307:1023-1034(2001).
-!- 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. {ECO:0000269|PubMed:10023679,
ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:11452037,
ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:11832948,
ECO:0000269|PubMed:12524539, ECO:0000269|PubMed:16617147,
ECO:0000269|PubMed:1719477, ECO:0000269|PubMed:18179823,
ECO:0000269|PubMed:18439621, ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:19401441, ECO:0000269|PubMed:19934257,
ECO:0000269|PubMed:20699270, ECO:0000269|PubMed:21496894,
ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:8355688,
ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:8932375,
ECO:0000269|PubMed:9108029, ECO:0000269|PubMed:9207062,
ECO:0000269|PubMed:9560228, ECO:0000269|PubMed:9804799}.
-!- 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. {ECO:0000255|PROSITE-ProRule:PRU00764,
ECO:0000269|PubMed:11286553, ECO:0000269|PubMed:15380100,
ECO:0000269|PubMed:19123919, ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11286553,
ECO:0000269|PubMed:19123919, ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11286553,
ECO:0000269|PubMed:19123919, ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799};
Note=Probably binds two magnesium or manganese ions per subunit.
{ECO:0000269|PubMed:11286553, ECO:0000269|PubMed:19123919,
ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799};
-!- 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: 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. {ECO:0000269|PubMed:10667800,
ECO:0000269|PubMed:11286553, ECO:0000269|PubMed:11809897,
ECO:0000269|PubMed:11909973, ECO:0000269|PubMed:12524539,
ECO:0000269|PubMed:14633989, ECO:0000269|PubMed:15942031,
ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:19219073, ECO:0000269|PubMed:19934257,
ECO:0000269|PubMed:20231292, ECO:0000269|PubMed:20699270,
ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9108029,
ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9351835}.
-!- INTERACTION:
Q09472:EP300; NbExp=8; IntAct=EBI-1048805, EBI-447295;
P08107:HSPA1B; NbExp=3; IntAct=EBI-1048805, EBI-629985;
Q96EB6:SIRT1; NbExp=6; IntAct=EBI-1048805, EBI-1802965;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. 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.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: 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. {ECO:0000250}.
-!- INDUCTION: Up-regulated in presence of reactive oxygen species
(ROS), like bleomycin, H(2)O(2) and phenazine methosulfate.
{ECO:0000269|PubMed:9560228}.
-!- 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.
-!- PTM: 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.
{ECO:0000269|PubMed:10023679, ECO:0000269|PubMed:11452037}.
-!- PTM: Acetylated on Lys-6 and Lys-7. Acetylation is increased by
the transcriptional coactivator EP300 acetyltransferase, genotoxic
agents like H(2)O(2) 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.
{ECO:0000269|PubMed:14633989, ECO:0000269|PubMed:20699270}.
-!- PTM: 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.
-!- PTM: Cys-65 and Cys-93 are nitrosylated in response to nitric
oxide (NO) and lead to the exposure of the nuclear export signal
(NES). {ECO:0000269|PubMed:17403694}.
-!- PTM: Ubiquitinated by MDM2; leading to translocation to the
cytoplasm and proteasomal degradation.
{ECO:0000269|PubMed:19219073}.
-!- 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/apex/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X59764; CAA42437.1; -; mRNA.
EMBL; M80261; AAA58371.1; -; mRNA.
EMBL; D90373; BAA14381.1; -; mRNA.
EMBL; S43127; AAB22977.1; -; mRNA.
EMBL; M81955; AAA58372.1; -; mRNA.
EMBL; M92444; AAA58629.1; -; Genomic_DNA.
EMBL; X66133; CAA46925.1; -; Genomic_DNA.
EMBL; D13370; BAA02633.1; -; Genomic_DNA.
EMBL; U79268; AAB50212.1; -; mRNA.
EMBL; BT007236; AAP35900.1; -; mRNA.
EMBL; AF488551; AAL86909.1; -; Genomic_DNA.
EMBL; AL355075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002338; AAH02338.1; -; mRNA.
EMBL; BC004979; AAH04979.1; -; mRNA.
EMBL; BC008145; AAH08145.1; -; mRNA.
EMBL; BC019291; AAH19291.1; -; mRNA.
EMBL; M99703; AAA58373.1; -; Genomic_DNA.
CCDS; CCDS9550.1; -.
PIR; S23550; S23550.
RefSeq; NP_001231178.1; NM_001244249.1.
RefSeq; NP_001632.2; NM_001641.3.
RefSeq; NP_542379.1; NM_080648.2.
RefSeq; NP_542380.1; NM_080649.2.
UniGene; Hs.73722; -.
PDB; 1BIX; X-ray; 2.20 A; A=32-318.
PDB; 1CQG; NMR; -; B=59-71.
PDB; 1CQH; NMR; -; B=59-71.
PDB; 1DE8; X-ray; 2.95 A; A/B=43-318.
PDB; 1DE9; X-ray; 3.00 A; A/B=43-318.
PDB; 1DEW; X-ray; 2.65 A; A/B=40-318.
PDB; 1E9N; X-ray; 2.20 A; A/B=2-318.
PDB; 1HD7; X-ray; 1.95 A; A=2-318.
PDB; 2ISI; X-ray; 2.76 A; A/B/C=2-318.
PDB; 2O3H; X-ray; 1.90 A; A=40-318.
PDB; 3U8U; X-ray; 2.15 A; A/B/C/D/E/F=1-318.
PDB; 4IEM; X-ray; 2.39 A; A/B/C/D=2-318.
PDB; 4LND; X-ray; 1.92 A; A/B/C=39-318.
PDB; 4QH9; X-ray; 2.18 A; A=38-318.
PDB; 4QHD; X-ray; 1.65 A; A=38-318.
PDB; 4QHE; X-ray; 1.40 A; A=38-318.
PDB; 5CFG; X-ray; 1.80 A; A=44-318.
PDB; 5DFF; X-ray; 1.57 A; A/B=43-318.
PDB; 5DFH; X-ray; 1.95 A; A/B=43-318.
PDB; 5DFI; X-ray; 1.63 A; A/B=43-318.
PDB; 5DFJ; X-ray; 1.85 A; A/B=43-318.
PDB; 5DG0; X-ray; 1.80 A; A/B=43-318.
PDBsum; 1BIX; -.
PDBsum; 1CQG; -.
PDBsum; 1CQH; -.
PDBsum; 1DE8; -.
PDBsum; 1DE9; -.
PDBsum; 1DEW; -.
PDBsum; 1E9N; -.
PDBsum; 1HD7; -.
PDBsum; 2ISI; -.
PDBsum; 2O3H; -.
PDBsum; 3U8U; -.
PDBsum; 4IEM; -.
PDBsum; 4LND; -.
PDBsum; 4QH9; -.
PDBsum; 4QHD; -.
PDBsum; 4QHE; -.
PDBsum; 5CFG; -.
PDBsum; 5DFF; -.
PDBsum; 5DFH; -.
PDBsum; 5DFI; -.
PDBsum; 5DFJ; -.
PDBsum; 5DG0; -.
DisProt; DP00007; -.
ProteinModelPortal; P27695; -.
SMR; P27695; -.
BioGrid; 106825; 87.
CORUM; P27695; -.
DIP; DIP-6130N; -.
IntAct; P27695; 45.
MINT; MINT-119189; -.
STRING; 9606.ENSP00000216714; -.
BindingDB; P27695; -.
ChEMBL; CHEMBL5619; -.
DrugBank; DB04967; Lucanthone.
iPTMnet; P27695; -.
PhosphoSitePlus; P27695; -.
SwissPalm; P27695; -.
BioMuta; APEX1; -.
DMDM; 113984; -.
EPD; P27695; -.
PaxDb; P27695; -.
PeptideAtlas; P27695; -.
PRIDE; P27695; -.
TopDownProteomics; P27695; -.
DNASU; 328; -.
Ensembl; ENST00000216714; ENSP00000216714; ENSG00000100823.
Ensembl; ENST00000398030; ENSP00000381111; ENSG00000100823.
Ensembl; ENST00000555414; ENSP00000451979; ENSG00000100823.
GeneID; 328; -.
KEGG; hsa:328; -.
UCSC; uc058yte.1; human.
CTD; 328; -.
DisGeNET; 328; -.
EuPathDB; HostDB:ENSG00000100823.11; -.
GeneCards; APEX1; -.
HGNC; HGNC:587; APEX1.
HPA; CAB004294; -.
HPA; CAB047307; -.
HPA; HPA000956; -.
HPA; HPA002564; -.
MalaCards; APEX1; -.
MIM; 107748; gene.
neXtProt; NX_P27695; -.
OpenTargets; ENSG00000100823; -.
PharmGKB; PA201059; -.
eggNOG; KOG1294; Eukaryota.
eggNOG; COG0708; LUCA.
GeneTree; ENSGT00530000063540; -.
HOGENOM; HOG000034586; -.
HOVERGEN; HBG050531; -.
InParanoid; P27695; -.
KO; K10771; -.
OMA; GTAVFTK; -.
OrthoDB; EOG091G0FDG; -.
PhylomeDB; P27695; -.
TreeFam; TF315048; -.
BRENDA; 4.2.99.18; 2681.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
Reactome; R-HSA-73933; Resolution of Abasic Sites (AP sites).
SIGNOR; P27695; -.
ChiTaRS; APEX1; human.
EvolutionaryTrace; P27695; -.
GeneWiki; APEX1; -.
GenomeRNAi; 328; -.
PMAP-CutDB; P27695; -.
PRO; PR:P27695; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100823; -.
CleanEx; HS_APEX1; -.
CleanEx; HS_HAP1; -.
ExpressionAtlas; P27695; baseline and differential.
Genevisible; P27695; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IC:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005840; C:ribosome; TAS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0008309; F:double-stranded DNA exodeoxyribonuclease activity; IDA:BHF-UCL.
GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0004520; F:endodeoxyribonuclease activity; TAS:Reactome.
GO; GO:0004519; F:endonuclease activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0004528; F:phosphodiesterase I activity; TAS:UniProtKB.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; TAS:UniProtKB.
GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0004844; F:uracil DNA N-glycosylase activity; TAS:ProtInc.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006284; P:base-excision repair; IDA:CAFA.
GO; GO:0006286; P:base-excision repair, base-free sugar-phosphate removal; TAS:Reactome.
GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0000723; P:telomere maintenance; IDA:BHF-UCL.
GO; GO:0097698; P:telomere maintenance via base-excision repair; IDA:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR004808; AP_endonuc_1.
InterPro; IPR020847; AP_endonuclease_F1_BS.
InterPro; IPR020848; AP_endonuclease_F1_CS.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
PANTHER; PTHR22748; PTHR22748; 1.
Pfam; PF03372; Exo_endo_phos; 1.
SUPFAM; SSF56219; SSF56219; 1.
TIGRFAMs; TIGR00633; xth; 1.
PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator;
Cleavage on pair of basic residues; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; DNA damage;
DNA recombination; DNA repair; DNA-binding; Endonuclease;
Endoplasmic reticulum; Exonuclease; Hydrolase; Lyase; Magnesium;
Metal-binding; Mitochondrion; Nuclease; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repressor; RNA-binding;
S-nitrosylation; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12524539,
ECO:0000269|PubMed:1380454}.
CHAIN 2 318 DNA-(apurinic or apyrimidinic site)
lyase.
/FTId=PRO_0000200010.
CHAIN 32 318 DNA-(apurinic or apyrimidinic site)
lyase, mitochondrial. {ECO:0000250}.
/FTId=PRO_0000402572.
REGION 2 33 Necessary for interaction with YBX1,
binding to RNA, NPM1-dependent
association with rRNA, endoribonuclease
activity on abasic RNA and localization
in the nucleoli.
{ECO:0000269|PubMed:18809583}.
REGION 23 33 Necessary for interaction with NPM1 and
for efficient rRNA binding.
REGION 289 318 Mitochondrial targeting sequence (MTS).
MOTIF 8 13 Nuclear localization signal (NLS).
MOTIF 64 80 Nuclear export signal (NES).
ACT_SITE 171 171
ACT_SITE 210 210 Proton donor/acceptor.
METAL 70 70 Magnesium 1.
METAL 96 96 Magnesium 1.
METAL 210 210 Magnesium 2.
METAL 212 212 Magnesium 2.
METAL 308 308 Magnesium 1.
SITE 31 32 Cleavage; by granzyme A.
SITE 212 212 Transition state stabilizer.
SITE 283 283 Important for catalytic activity.
SITE 309 309 Interaction with DNA substrate.
MOD_RES 6 6 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:14633989}.
MOD_RES 7 7 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:14633989}.
MOD_RES 27 27 N6-acetyllysine.
{ECO:0000269|PubMed:20699270}.
MOD_RES 31 31 N6-acetyllysine.
{ECO:0000269|PubMed:20699270}.
MOD_RES 32 32 N6-acetyllysine.
{ECO:0000269|PubMed:20699270}.
MOD_RES 35 35 N6-acetyllysine.
{ECO:0000269|PubMed:20699270}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 65 65 S-nitrosocysteine; alternate.
{ECO:0000269|PubMed:17403694}.
MOD_RES 93 93 S-nitrosocysteine; alternate.
{ECO:0000269|PubMed:17403694}.
MOD_RES 197 197 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 233 233 Phosphothreonine; by CDK5.
{ECO:0000250|UniProtKB:P28352}.
MOD_RES 310 310 S-nitrosocysteine.
{ECO:0000269|PubMed:17403694}.
DISULFID 65 93 Alternate. {ECO:0000305}.
VARIANT 51 51 Q -> H (in dbSNP:rs1048945).
{ECO:0000269|Ref.11}.
/FTId=VAR_013455.
VARIANT 64 64 I -> V (in dbSNP:rs2307486).
{ECO:0000269|Ref.11}.
/FTId=VAR_014823.
VARIANT 148 148 D -> E (in dbSNP:rs1130409).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.11}.
/FTId=VAR_019790.
MUTAGEN 6 6 K->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.
{ECO:0000269|PubMed:14633989,
ECO:0000269|PubMed:15942031,
ECO:0000269|PubMed:18809583,
ECO:0000269|PubMed:19934257}.
MUTAGEN 7 7 K->R: Lack of acetylation and does not
stimulate the YBX1-mediated MDR1 promoter
activity and alter nuclear subcellular
localization; when associated with R-6.
{ECO:0000269|PubMed:14633989,
ECO:0000269|PubMed:15942031,
ECO:0000269|PubMed:18809583,
ECO:0000269|PubMed:19934257}.
MUTAGEN 12 12 E->A: Reduces nuclear localization; when
associated with A-13.
{ECO:0000269|PubMed:15942031}.
MUTAGEN 13 13 D->A: Reduces nuclear localization; when
associated with A-12.
{ECO:0000269|PubMed:15942031}.
MUTAGEN 24 24 K->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.
{ECO:0000269|PubMed:19219073,
ECO:0000269|PubMed:20231292,
ECO:0000269|PubMed:20699270}.
MUTAGEN 25 25 K->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.
{ECO:0000269|PubMed:19219073,
ECO:0000269|PubMed:20231292,
ECO:0000269|PubMed:20699270}.
MUTAGEN 27 27 K->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.
{ECO:0000269|PubMed:19219073,
ECO:0000269|PubMed:20231292,
ECO:0000269|PubMed:20699270}.
MUTAGEN 31 31 K->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.
{ECO:0000269|PubMed:12524539,
ECO:0000269|PubMed:20231292,
ECO:0000269|PubMed:20699270}.
MUTAGEN 32 32 K->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.
{ECO:0000269|PubMed:20699270}.
MUTAGEN 65 65 C->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. {ECO:0000269|PubMed:12524539,
ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 65 65 C->S: Does not abolish NO-induced
nitrosylation. Enhances NO-induced
nuclear export.
{ECO:0000269|PubMed:12524539,
ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 68 68 N->A: Nearly abolishes AP
endodeoxyribonuclease activity.
{ECO:0000269|PubMed:21762700}.
MUTAGEN 70 70 D->A: Strongly reduces AP
endodeoxyribonuclease activity.
{ECO:0000269|PubMed:21762700}.
MUTAGEN 93 93 C->A: Abolishes partially the redox
activity. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 93 93 C->S: Does not abolish NO-induced
nitrosylation. Abolishes NO-induced
nitrosylation and translocation from the
nucleus to the cytoplasm; when associated
with S-310. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 96 96 E->A: Lacks MYC CRD RNA cleavage
activity. {ECO:0000269|PubMed:19401441}.
MUTAGEN 99 99 C->A: Does not abolish the redox
activity. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 138 138 C->A: Does not abolish the redox
activity. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 171 171 Y->A,F,H: Abolishes the AP
endodeoxyribonuclease activity.
{ECO:0000269|PubMed:15380100,
ECO:0000269|PubMed:21762700}.
MUTAGEN 208 208 C->A: Does not abolish the redox
activity. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 210 210 D->A,N: Abolishes the AP
endodeoxyribonuclease activity. Reduces
protection from granzyme A-mediated cell
death; when associated with A-31 and A-
65. {ECO:0000269|PubMed:12524539}.
MUTAGEN 212 212 N->A: Abolishes AP endodeoxyribonuclease
activity. {ECO:0000269|PubMed:8932375}.
MUTAGEN 212 212 N->Q,D: Decreases AP
endodeoxyribonuclease activity.
{ECO:0000269|PubMed:8932375}.
MUTAGEN 266 266 F->A: Strongly reduces AP
endodeoxyribonuclease activity.
{ECO:0000269|PubMed:21762700}.
MUTAGEN 283 283 D->A: Strongly reduces AP
endodeoxyribonuclease activity, but does
not affect RNA cleavage activity. Nearly
abolishes AP endodeoxyribonuclease
activity; when associated with A-308.
{ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799}.
MUTAGEN 296 296 C->A: Does not abolish the redox
activity. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 299 299 K->A: Reduces the interaction with
TOMM20. Abolishes localization in the
mitochondria; when associated with A-301.
{ECO:0000269|PubMed:20231292}.
MUTAGEN 301 301 R->A: Reduces the interaction with
TOMM20. Abolishes localization in the
mitochondria; when associated with A-299.
{ECO:0000269|PubMed:20231292}.
MUTAGEN 303 303 K->A: Reduces the interaction with
TOMM20. {ECO:0000269|PubMed:20231292}.
MUTAGEN 308 308 D->A: Reduces AP endodeoxyribonuclease
activity. Nearly abolishes AP
endodeoxyribonuclease activity; when
associated with A-283.
{ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799}.
MUTAGEN 309 309 H->N,S: Abolishes AP
endodeoxyribonuclease activity. Lacks MYC
CRD RNA cleavage activity.
{ECO:0000269|PubMed:19401441,
ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799}.
MUTAGEN 310 310 C->A: Does not abolish the redox
activity. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
MUTAGEN 310 310 C->S: Does not abolish NO-induced
nitrosylation. Abolishes NO-induced
nitrosylation and translocation from the
nucleus to the cytoplasm; when associated
with S-93. {ECO:0000269|PubMed:18579163,
ECO:0000269|PubMed:8355688}.
CONFLICT 57 57 G -> A (in Ref. 2; AAA58371).
{ECO:0000305}.
CONFLICT 306 306 G -> A (in Ref. 2; AAA58371).
{ECO:0000305}.
STRAND 62 68 {ECO:0000244|PDB:4QHE}.
HELIX 72 77 {ECO:0000244|PDB:4QHE}.
HELIX 80 87 {ECO:0000244|PDB:4QHE}.
STRAND 90 95 {ECO:0000244|PDB:4QHE}.
HELIX 101 103 {ECO:0000244|PDB:5DFF}.
HELIX 106 110 {ECO:0000244|PDB:4QHE}.
HELIX 112 114 {ECO:0000244|PDB:4QHE}.
STRAND 116 120 {ECO:0000244|PDB:4QHE}.
STRAND 123 125 {ECO:0000244|PDB:5DFJ}.
STRAND 127 129 {ECO:0000244|PDB:4QHE}.
STRAND 131 137 {ECO:0000244|PDB:4QHE}.
STRAND 140 145 {ECO:0000244|PDB:4QHE}.
HELIX 149 151 {ECO:0000244|PDB:4QHE}.
STRAND 152 154 {ECO:0000244|PDB:4QHE}.
STRAND 157 161 {ECO:0000244|PDB:4QHE}.
STRAND 166 171 {ECO:0000244|PDB:4QHE}.
HELIX 177 179 {ECO:0000244|PDB:4QHE}.
HELIX 182 200 {ECO:0000244|PDB:4QHE}.
STRAND 205 210 {ECO:0000244|PDB:4QHE}.
HELIX 217 219 {ECO:0000244|PDB:4QHE}.
TURN 224 228 {ECO:0000244|PDB:4QHE}.
TURN 230 232 {ECO:0000244|PDB:1DEW}.
HELIX 234 246 {ECO:0000244|PDB:4QHE}.
STRAND 249 251 {ECO:0000244|PDB:2ISI}.
HELIX 252 256 {ECO:0000244|PDB:4QHE}.
STRAND 257 259 {ECO:0000244|PDB:1DE9}.
HELIX 270 272 {ECO:0000244|PDB:5DFI}.
HELIX 273 276 {ECO:0000244|PDB:4QHE}.
STRAND 283 287 {ECO:0000244|PDB:4QHE}.
HELIX 289 294 {ECO:0000244|PDB:4QHE}.
STRAND 295 300 {ECO:0000244|PDB:4QHE}.
STRAND 306 309 {ECO:0000244|PDB:4QHE}.
STRAND 312 316 {ECO:0000244|PDB:4QHE}.
SEQUENCE 318 AA; 35555 MW; B88579C01BAF80C6 CRC64;
MPKRGKKGAV AEDGDELRTE PEAKKSKTAA KKNDKEAAGE GPALYEDPPD QKTSPSGKPA
TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS ENKLPAELQE LPGLSHQYWS
APSDKEGYSG VGLLSRQCPL KVSYGIGDEE HDQEGRVIVA EFDSFVLVTA YVPNAGRGLV
RLEYRQRWDE AFRKFLKGLA SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF
GELLQAVPLA DSFRHLYPNT PYAYTFWTYM MNARSKNVGW RLDYFLLSHS LLPALCDSKI
RSKALGSDHC PITLYLAL


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