LOCUS NP_542379 318 aa linear PRI 04-JAN-2024
DEFINITION DNA-(apurinic or apyrimidinic site) endonuclease [Homo sapiens].
ACCESSION NP_542379
VERSION NP_542379.1
DBSOURCE REFSEQ: accession NM_080648.3
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 318)
AUTHORS Bakman AS, Boichenko SS, Kuznetsova AA, Ishchenko AA, Saparbaev M
and Kuznetsov NA.
TITLE Coordination between human DNA polymerase beta and
apurinic/apyrimidinic endonuclease 1 in the course of DNA repair
JOURNAL Biochimie 216, 126-136 (2024)
PUBMED 37806619
REMARK GeneRIF: Coordination between human DNA polymerase beta and
apurinic/apyrimidinic endonuclease 1 in the course of DNA repair.
REFERENCE 2 (residues 1 to 318)
AUTHORS Gautam A, Fawcett H, Burdova K, Brazina J and Caldecott KW.
TITLE APE1-dependent base excision repair of DNA photodimers in human
cells
JOURNAL Mol Cell 83 (20), 3669-3678 (2023)
PUBMED 37816354
REMARK GeneRIF: APE1-dependent base excision repair of DNA photodimers in
human cells.
REFERENCE 3 (residues 1 to 318)
AUTHORS Tabanifar B, Moorthy A, Tsai HH, Kannan S, Verma CS and Sabapathy
K.
TITLE JNK mediates cell death by promoting the ubiquitination of the
apurinic/apyrimidinic endonuclease APE1
JOURNAL Cell Rep 42 (9), 113123 (2023)
PUBMED 37703179
REMARK GeneRIF: JNK mediates cell death by promoting the ubiquitination of
the apurinic/apyrimidinic endonuclease APE1.
REFERENCE 4 (residues 1 to 318)
AUTHORS Hong JY, Oh HH, Park SY, Park YL, Cho SB and Joo YE.
TITLE Expression of Apurinic/Apyrimidinic Endonuclease 1 in Colorectal
Cancer and its Relation to Tumor Progression and Prognosis
JOURNAL In Vivo 37 (5), 2070-2077 (2023)
PUBMED 37652525
REMARK GeneRIF: Expression of Apurinic/Apyrimidinic Endonuclease 1 in
Colorectal Cancer and its Relation to Tumor Progression and
Prognosis.
REFERENCE 5 (residues 1 to 318)
AUTHORS Liu L, Wu Q, Wang Z, Niu B, Jiao Y and An H.
TITLE APE1 promotes embryonic stem cell proliferation and teratoma
formation by regulating GDNF/GFRalpha1 axis
JOURNAL Reprod Biol 23 (3), 100792 (2023)
PUBMED 37523789
REMARK GeneRIF: APE1 promotes embryonic stem cell proliferation and
teratoma formation by regulating GDNF/GFRalpha1 axis.
REFERENCE 6 (residues 1 to 318)
AUTHORS Harrison L, Ascione G, Menninger JC, Ward DC and Demple B.
TITLE Human apurinic endonuclease gene (APE): structure and genomic
mapping (chromosome 14q11.2-12)
JOURNAL Hum Mol Genet 1 (9), 677-680 (1992)
PUBMED 1284593
REFERENCE 7 (residues 1 to 318)
AUTHORS Robson CN, Hochhauser D, Craig R, Rack K, Buckle VJ and Hickson ID.
TITLE Structure of the human DNA repair gene HAP1 and its localisation to
chromosome 14q 11.2-12
JOURNAL Nucleic Acids Res 20 (17), 4417-4421 (1992)
PUBMED 1383925
REFERENCE 8 (residues 1 to 318)
AUTHORS Xanthoudakis S, Miao G, Wang F, Pan YC and Curran T.
TITLE Redox activation of Fos-Jun DNA binding activity is mediated by a
DNA repair enzyme
JOURNAL EMBO J 11 (9), 3323-3335 (1992)
PUBMED 1380454
REFERENCE 9 (residues 1 to 318)
AUTHORS Zhao B, Grandy DK, Hagerup JM, Magenis RE, Smith L, Chauhan BC and
Henner WD.
TITLE The human gene for apurinic/apyrimidinic endonuclease (HAP1):
sequence and localization to chromosome 14 band q12
JOURNAL Nucleic Acids Res 20 (15), 4097-4098 (1992)
PUBMED 1380694
REFERENCE 10 (residues 1 to 318)
AUTHORS Cheng XB, Bunville J and Patterson TA.
TITLE Nucleotide sequence of a cDNA for an apurinic/apyrimidinic
endonuclease from HeLa cells
JOURNAL Nucleic Acids Res 20 (2), 370 (1992)
PUBMED 1371347
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AL355075.6 and BC004979.1.
Summary: The APEX gene encodes the major AP endonuclease in human
cells. It encodes the APEX endonuclease, a DNA repair enzyme with
apurinic/apyrimidinic (AP) activity. Such AP activity sites occur
frequently in DNA molecules by spontaneous hydrolysis, by DNA
damaging agents or by DNA glycosylases that remove specific
abnormal bases. The AP sites are the most frequent pre-mutagenic
lesions that can prevent normal DNA replication. Splice variants
have been found for this gene; all encode the same protein.
Disruptions in the biological functions related to APEX are
associated with many various malignancies and neurodegenerative
diseases.[provided by RefSeq, Dec 2019].
Transcript Variant: This variant (2) uses a different donor splice
site for exon 1 when compared to variant 1.
Sequence Note: This RefSeq record was created from transcript and
genomic sequence data to make the sequence consistent with the
reference genome assembly. The genomic coordinates used for the
transcript record were based on transcript alignments.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR7346977.126332.1, BC004979.1
[ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA1968540, SAMEA1970526
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
gene product(s) localized to mito. :: inferred from homology
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..318
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="14"
/map="14q11.2"
Protein 1..318
/product="DNA-(apurinic or apyrimidinic site)
endonuclease"
/EC_number="3.1.11.2"
/note="AP endonuclease class I; deoxyribonuclease
(apurinic or apyrimidinic); AP lyase; DNA-(apurinic or
apyrimidinic site) lyase; apurinic/apyrimidinic (abasic)
endonuclease; protein REF-1; apurinic-apyrimidinic
endonuclease 1; redox factor-1; APEX nuclease
(multifunctional DNA repair enzyme) 1"
/calculated_mol_wt=35423
Region 1..60
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
Region 2..33
/region_name="Necessary for interaction with YBX1, binding
to RNA, NPM1-dependent association with rRNA,
endoribonuclease activity on abasic RNA and localization
in the nucleoli. /evidence=ECO:0000269|PubMed:18809583"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
Site 6
/site_type="acetylation"
/note="N6-acetyllysine, by EP300.
/evidence=ECO:0000269|PubMed:14633989; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 7
/site_type="acetylation"
/note="N6-acetyllysine, by EP300.
/evidence=ECO:0000269|PubMed:14633989; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Region 8..13
/region_name="Nuclear localization signal (NLS)"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
Region 23..33
/region_name="Necessary for interaction with NPM1 and for
efficient rRNA binding"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
Site 27
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000269|PubMed:20699270; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 31..32
/site_type="cleavage"
/note="Cleavage, by granzyme A; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 31
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000269|PubMed:20699270; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
mat_peptide 32..318
/product="DNA-(apurinic or apyrimidinic site)
endonuclease, mitochondrial. /evidence=ECO:0000250.
/id=PRO_0000402572"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
/calculated_mol_wt=32245
Site 32
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000269|PubMed:20699270; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 35
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000269|PubMed:20699270; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 54
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Region 64..80
/region_name="Nuclear export signal (NES)"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
Site 197
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0007744|PubMed:19608861; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 212
/site_type="other"
/note="Transition state stabilizer.
/evidence=ECO:0000269|PubMed:8932375; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 233
/site_type="phosphorylation"
/note="Phosphothreonine, by CDK5.
/evidence=ECO:0000250|UniProtKB:P28352; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Site 283
/site_type="other"
/note="Important for catalytic activity.
/evidence=ECO:0000269|PubMed:21762700,
ECO:0000269|PubMed:9804799; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
Region 289..318
/region_name="Mitochondrial targeting sequence (MTS)"
/note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
Site 309
/site_type="other"
/note="Interaction with DNA substrate; propagated from
UniProtKB/Swiss-Prot (P27695.2)"
CDS 1..318
/gene="APEX1"
/gene_synonym="APE; APE1; APEN; APEX; APX; HAP1; REF1"
/coded_by="NM_080648.3:172..1128"
/db_xref="CCDS:CCDS9550.1"
/db_xref="GeneID:328"
/db_xref="HGNC:HGNC:587"
/db_xref="MIM:107748"
ORIGIN
1 mpkrgkkgav aedgdelrte peakksktaa kkndkeaage gpalyedppd qktspsgkpa
61 tlkicswnvd glrawikkkg ldwvkeeapd ilclqetkcs enklpaelqe lpglshqyws
121 apsdkegysg vgllsrqcpl kvsygigdee hdqegrviva efdsfvlvta yvpnagrglv
181 rleyrqrwde afrkflkgla srkplvlcgd lnvaheeidl rnpkgnkkna gftpqerqgf
241 gellqavpla dsfrhlypnt pyaytfwtym mnarsknvgw rldyfllshs llpalcdski
301 rskalgsdhc pitlylal
//
