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DNA-(apurinic or apyrimidinic site) lyase



Homo sapiens (Human)
Reviewed-Annotation score: -Experimental evidence at protein leveli


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.25 Publications


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.By similarity

Catalytic activityi

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.PROSITE-ProRule annotation5 Publications


Mg2+4 Publications, Mn2+4 PublicationsNote: Probably binds two magnesium or manganese ions per subunit.4 Publications

Enzyme regulationi

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


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi70Magnesium 11
Metal bindingi96Magnesium 11
Active sitei1711
Active sitei210Proton donor/acceptor1
Metal bindingi210Magnesium 21
Metal bindingi212Magnesium 21
Sitei212Transition state stabilizer1
Sitei283Important for catalytic activity1
Metal bindingi308Magnesium 11

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • class I DNA-(apurinic or apyrimidinic site) endonuclease activity Source: UniProtKB-EC
  • damaged DNA binding Source: UniProtKB
  • DNA-(apurinic or apyrimidinic site) endonuclease activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: GO_Central
  • double-stranded DNA exodeoxyribonuclease activity Source: BHF-UCL
  • double-stranded telomeric DNA binding Source: BHF-UCL
  • endodeoxyribonuclease activity Source: Reactome
  • endonuclease activity Source: MGI
  • metal ion binding Source: UniProtKB
  • NF-kappaB binding Source: Ensembl
  • oxidoreductase activity Source: UniProtKB
  • phosphodiesterase I activity Source: UniProtKB
  • phosphoric diester hydrolase activity Source: UniProtKB
  • protein-containing complex binding Source: Ensembl
  • RNA binding Source: UniProtKB
  • RNA-DNA hybrid ribonuclease activity Source: UniProtKB
  • site-specific endodeoxyribonuclease activity, specific for altered base Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: ProtInc
  • uracil DNA N-glycosylase activity Source: ProtInc

GO - Biological processi

  • aging Source: Ensembl
  • base-excision repair Source: CAFA
  • base-excision repair, base-free sugar-phosphate removal Source: Reactome
  • cell redox homeostasis Source: Ensembl
  • cellular response to cAMP Source: Ensembl
  • cellular response to hydrogen peroxide Source: Ensembl
  • cellular response to peptide hormone stimulus Source: Ensembl
  • DNA demethylation Source: UniProtKB
  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: UniProtKB
  • negative regulation of smooth muscle cell migration Source: Ensembl
  • positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • regulation of apoptotic process Source: UniProtKB
  • regulation of mRNA stability Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • telomere maintenance Source: BHF-UCL
  • telomere maintenance via base-excision repair Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW


Molecular functionActivator, DNA-binding, Endonuclease, Exonuclease, Hydrolase, Lyase, Nuclease, Repressor, RNA-binding
Biological processDNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.99.18 2681
ReactomeiR-HSA-110357 Displacement of DNA glycosylase by APEX1
R-HSA-110362 POLB-Dependent Long Patch Base Excision Repair
R-HSA-110373 Resolution of AP sites via the multiple-nucleotide patch replacement pathway
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-73930 Abasic sugar-phosphate removal via the single-nucleotide replacement pathway
R-HSA-73933 Resolution of Abasic Sites (AP sites)

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-(apurinic or apyrimidinic site) lyase (EC:3.1.-.-, EC:
Alternative name(s):
APEX nuclease
Short name:
Apurinic-apyrimidinic endonuclease 1
Short name:
AP endonuclease 1
Short name:
Redox factor-1
Cleaved into the following chain:
Gene namesi
Synonyms:APE, APE1, APEX, APX, HAP1, REF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

MIMi107748 gene

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6K → 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. 4 Publications1
Mutagenesisi7K → R: Lack of acetylation and does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-6. 4 Publications1
Mutagenesisi12E → A: Reduces nuclear localization; when associated with A-13. 1 Publication1
Mutagenesisi13D → A: Reduces nuclear localization; when associated with A-12. 1 Publication1
Mutagenesisi24K → 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. 3 Publications1
Mutagenesisi25K → 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. 3 Publications1
Mutagenesisi27K → 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. 3 Publications1
Mutagenesisi31K → 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. 3 Publications1
Mutagenesisi32K → 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. 1 Publication1
Mutagenesisi65C → 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. 3 Publications1
Mutagenesisi65C → S: Does not abolish NO-induced nitrosylation. Enhances NO-induced nuclear export. 3 Publications1
Mutagenesisi68N → A: Nearly abolishes AP endodeoxyribonuclease activity. 1 Publication1
Mutagenesisi70D → A: Strongly reduces AP endodeoxyribonuclease activity. 1 Publication1
Mutagenesisi93C → A: Abolishes partially the redox activity. 2 Publications1
Mutagenesisi93C → S: Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-310. 2 Publications1
Mutagenesisi96E → A: Lacks MYC CRD RNA cleavage activity. 1 Publication1
Mutagenesisi99C → A: Does not abolish the redox activity. 2 Publications1
Mutagenesisi138C → A: Does not abolish the redox activity. 2 Publications1
Mutagenesisi171Y → A, F or H: Abolishes the AP endodeoxyribonuclease activity. 2 Publications1
Mutagenesisi208C → A: Does not abolish the redox activity. 2 Publications1
Mutagenesisi210D → A or N: Abolishes the AP endodeoxyribonuclease activity. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-65. 1 Publication1
Mutagenesisi212N → A: Abolishes AP endodeoxyribonuclease activity. 1 Publication1
Mutagenesisi212N → Q or D: Decreases AP endodeoxyribonuclease activity. 1 Publication1
Mutagenesisi266F → A: Strongly reduces AP endodeoxyribonuclease activity. 1 Publication1
Mutagenesisi283D → A: Strongly reduces AP endodeoxyribonuclease activity, but does not affect RNA cleavage activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-308. 2 Publications1
Mutagenesisi296C → A: Does not abolish the redox activity. 2 Publications1
Mutagenesisi299K → A: Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-301. 1 Publication1
Mutagenesisi301R → A: Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-299. 1 Publication1
Mutagenesisi303K → A: Reduces the interaction with TOMM20. 1 Publication1
Mutagenesisi308D → A: Reduces AP endodeoxyribonuclease activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-283. 2 Publications1
Mutagenesisi309H → N or S: Abolishes AP endodeoxyribonuclease activity. Lacks MYC CRD RNA cleavage activity. 3 Publications1
Mutagenesisi310C → A: Does not abolish the redox activity. 2 Publications1
Mutagenesisi310C → S: Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-93. 2 Publications1

Organism-specific databases


Chemistry databases

DrugBankiDB04967 Lucanthone

Polymorphism and mutation databases


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002000102 – 318DNA-(apurinic or apyrimidinic site) lyaseAdd BLAST317
ChainiPRO_000040257232 – 318DNA-(apurinic or apyrimidinic site) lyase, mitochondrialBy similarityAdd BLAST287

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6N6-acetyllysine; by EP3001 Publication1
Modified residuei7N6-acetyllysine; by EP3001 Publication1
Modified residuei27N6-acetyllysine1 Publication1
Modified residuei31N6-acetyllysine1 Publication1
Modified residuei32N6-acetyllysine1 Publication1
Modified residuei35N6-acetyllysine1 Publication1
Modified residuei54PhosphoserineCombined sources1
Disulfide bondi65 ↔ 93AlternateCurated
Modified residuei65S-nitrosocysteine; alternate1 Publication1
Modified residuei93S-nitrosocysteine; alternate1 Publication1
Modified residuei197N6-acetyllysineCombined sources1
Modified residuei233Phosphothreonine; by CDK5By similarity1
Modified residuei310S-nitrosocysteine1 Publication1

Post-translational modificationi

Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death.2 Publications
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 SIRT1.2 Publications
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).1 Publication
Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation.1 Publication


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei31 – 32Cleavage; by granzyme A2

Keywords - PTMi

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

Proteomic databases


PTM databases


Miscellaneous databases




Up-regulated in presence of reactive oxygen species (ROS), like bleomycin, H2O2 and phenazine methosulfate.1 Publication

Gene expression databases

ExpressionAtlasiP27695 baseline and differential
GenevisibleiP27695 HS

Organism-specific databases



Subunit structurei

Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed of at least APEX1, SET, ANP32A, HMGB2, NME1 and TREX1. Associates with the dimer XRCC5/XRCC6 in a DNA-dependent manner. Interacts with SIRT1; the interaction is increased in the context of genotoxic stress. Interacts with HDAC1, HDAC2 and HDAC3; the interactions are not dependent on the APEX1 acetylation status. Interacts with XRCC1; the interaction is induced by SIRT1 and increased with the APEX1 acetylated form. Interacts with NPM1 (via N-terminal domain); the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts (via N-terminus) with YBX1 (via C-terminus); the interaction is increased in presence of APEX1 acetylated at Lys-6 and Lys-7. Interacts with HNRNPL; the interaction is DNA-dependent. Interacts (via N-terminus) with KPNA1 and KPNA2. Interacts with TXN; the interaction stimulates the FOS/JUN AP-1 complex DNA-binding activity in a redox-dependent manner. Interacts with GZMA, KRT8, MDM2, POLB, PRDX6, PRPF19, RPLP0, TOMM20 and WDR77. Binds to CDK5.17 Publications


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei309Interaction with DNA substrate1

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi106825, 90 interactors
IntActiP27695, 48 interactors

Chemistry databases



Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi62 – 68Combined sources7
Helixi72 – 77Combined sources6
Helixi80 – 87Combined sources8
Beta strandi90 – 95Combined sources6
Helixi101 – 103Combined sources3
Helixi106 – 110Combined sources5
Helixi112 – 114Combined sources3
Beta strandi116 – 120Combined sources5
Beta strandi123 – 125Combined sources3
Beta strandi127 – 129Combined sources3
Beta strandi131 – 137Combined sources7
Beta strandi140 – 145Combined sources6
Helixi149 – 151Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi157 – 161Combined sources5
Beta strandi166 – 171Combined sources6
Helixi177 – 179Combined sources3
Helixi182 – 200Combined sources19
Beta strandi205 – 210Combined sources6
Helixi217 – 219Combined sources3
Turni224 – 228Combined sources5
Turni230 – 232Combined sources3
Helixi234 – 246Combined sources13
Beta strandi249 – 251Combined sources3
Helixi252 – 256Combined sources5
Beta strandi257 – 259Combined sources3
Helixi270 – 272Combined sources3
Helixi273 – 276Combined sources4
Beta strandi283 – 287Combined sources5
Helixi289 – 294Combined sources6
Beta strandi295 – 300Combined sources6
Beta strandi306 – 309Combined sources4
Beta strandi312 – 316Combined sources5

3D structure databases


Miscellaneous databases


Family & Domainsi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 33Necessary for interaction with YBX1, binding to RNA, NPM1-dependent association with rRNA, endoribonuclease activity on abasic RNA and localization in the nucleoli1 PublicationAdd BLAST32
Regioni23 – 33Necessary for interaction with NPM1 and for efficient rRNA bindingAdd BLAST11
Regioni289 – 318Mitochondrial targeting sequence (MTS)Add BLAST30


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi8 – 13Nuclear localization signal (NLS)6
Motifi64 – 80Nuclear export signal (NES)Add BLAST17


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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1294 Eukaryota

Family and domain databases

Gene3Di3.60.10.10, 1 hit
InterProiView protein in InterPro
IPR004808 AP_endonuc_1
IPR020847 AP_endonuclease_F1_BS
IPR020848 AP_endonuclease_F1_CS
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
PANTHERiPTHR22748 PTHR22748, 1 hit
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
SUPFAMiSSF56219 SSF56219, 1 hit
TIGRFAMsiTIGR00633 xth, 1 hit
PROSITEiView protein in PROSITE
PS00726 AP_NUCLEASE_F1_1, 1 hit
PS00727 AP_NUCLEASE_F1_2, 1 hit
PS00728 AP_NUCLEASE_F1_3, 1 hit
PS51435 AP_NUCLEASE_F1_4, 1 hit


Sequence statusi: Complete.

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

P27695-1 [UniParc]FASTAAdd to basket

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Mass (Da):35,555
Last modified:January 23, 2007 - v2

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti57G → A in AAA58371 (PubMed:1722334).Curated1
Sequence conflicti306G → A in AAA58371 (PubMed:1722334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01345551Q → H1 PublicationCorresponds to variant dbSNP:rs1048945Ensembl.1
Natural variantiVAR_01482364I → V1 PublicationCorresponds to variant dbSNP:rs2307486Ensembl.1
Natural variantiVAR_019790148D → E2 PublicationsCorresponds to variant dbSNP:rs1130409Ensembl.1

Sequence databases

Select the link destinations:
Links Updated
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
RefSeqiNP_001231178.1, NM_001244249.1
NP_001632.2, NM_001641.3
NP_542379.1, NM_080648.2
NP_542380.1, NM_080649.2

Genome annotation databases

EnsembliENST00000216714; ENSP00000216714; ENSG00000100823
ENST00000398030; ENSP00000381111; ENSG00000100823
ENST00000555414; ENSP00000451979; ENSG00000100823
UCSCiuc058yte.1 human

Keywords - Coding sequence diversityi


Similar proteinsi

Entry informationi

Entry nameiAPEX1_HUMAN
AccessioniPrimary (citable) accession number: P27695
Secondary accession number(s): Q969L5, Q99775
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 224 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.


Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome


  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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