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UniProtKB - P27695 (APEX1_HUMAN)

Entry version 236 (18 Sep 2019)
Sequence version 2 (23 Jan 2007)
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Protein

DNA-(apurinic or apyrimidinic site) lyase

Gene

APEX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are 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

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.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi70Magnesium 11
Metal bindingi96Magnesium 11
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1711
Active sitei210Proton donor/acceptor1
Metal bindingi210Magnesium 21
Metal bindingi212Magnesium 21
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei212Transition state stabilizer1
Sitei283Important for catalytic activity1
Metal bindingi308Magnesium 11

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.2.99.18 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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)

SIGNOR Signaling Network Open Resource

More...SIGNORi		P27695

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-(apurinic or apyrimidinic site) lyase (EC:3.1.-.-, EC:4.2.99.18)
Alternative name(s):
APEX nuclease
Short name:
APEN
Apurinic-apyrimidinic endonuclease 1
Short name:
AP endonuclease 1
Short name:
APE-1
REF-1
Redox factor-1
Cleaved into the following chain:
DNA-(apurinic or apyrimidinic site) lyase, mitochondrial
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:APEX1
Synonyms:APE, APE1, APEX, APX, HAP1, REF1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:587 APEX1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		107748 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P27695

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		328

Open Targets

More...OpenTargetsi		ENSG00000100823

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA201059

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5619

Drug and drug target database

More...DrugBanki		DB04967 Lucanthone

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		APEX1

Domain mapping of disease mutations (DMDM)

More...DMDMi		113984

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

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

The CPTAC Assay portal

More...CPTACi		CPTAC-23
CPTAC-24

Encyclopedia of Proteome Dynamics

More...EPDi		P27695

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P27695

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P27695

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P27695

PeptideAtlas

More...PeptideAtlasi		P27695

PRoteomics IDEntifications database

More...PRIDEi		P27695

ProteomicsDB human proteome resource

More...ProteomicsDBi		54406

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P27695

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P27695

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P27695

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P27695

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P27695

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000100823 Expressed in 229 organ(s), highest expression level in embryo

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P27695 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P27695 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004294
CAB047307
HPA000956
HPA002564

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei309Interaction with DNA substrate1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		106825, 105 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P27695

Database of interacting proteins

More...DIPi		DIP-6130N

Protein interaction database and analysis system

More...IntActi		P27695, 47 interactors

Molecular INTeraction database

More...MINTi		P27695

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000216714

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P27695

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P27695

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P27695

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi8 – 13Nuclear localization signal (NLS)6
Motifi64 – 80Nuclear export signal (NES)Add BLAST17

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1294 Eukaryota
COG0708 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063540

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000034586

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P27695

KEGG Orthology (KO)

More...KOi		K10771

Identification of Orthologs from Complete Genome Data

More...OMAi		GTAVFTK

Database of Orthologous Groups

More...OrthoDBi		1105625at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P27695

TreeFam database of animal gene trees

More...TreeFami		TF315048

Family and domain databases

Database of protein disorder

More...DisProti		DP00007

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View 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

The PANTHER Classification System

More...PANTHERi		PTHR22748 PTHR22748, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03372 Exo_endo_phos, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56219 SSF56219, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00633 xth, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 11 potential isoforms that are computationally mapped.Show allAlign All

P27695-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKRGKKGAV AEDGDELRTE PEAKKSKTAA KKNDKEAAGE GPALYEDPPD 
        60         70         80         90        100
QKTSPSGKPA TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS 
       110        120        130        140        150
ENKLPAELQE LPGLSHQYWS APSDKEGYSG VGLLSRQCPL KVSYGIGDEE 
       160        170        180        190        200
HDQEGRVIVA EFDSFVLVTA YVPNAGRGLV RLEYRQRWDE AFRKFLKGLA 
       210        220        230        240        250
SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF GELLQAVPLA 
       260        270        280        290        300
DSFRHLYPNT PYAYTFWTYM MNARSKNVGW RLDYFLLSHS LLPALCDSKI 
       310 
RSKALGSDHC PITLYLAL
Length:318
Mass (Da):35,555
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB88579C01BAF80C6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 11 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V3M6G3V3M6_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
263Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5Q1G3V5Q1_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
242Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V359G3V359_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
172Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V3C7G3V3C7_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
174Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5M0G3V5M0_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
162Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0C4DGK8A0A0C4DGK8_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
146Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C4A8H7C4A8_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
150Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5D9G3V5D9_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
107Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V2D9G3V2D9_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
49Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V3Y6G3V3Y6_HUMAN
DNA-(apurinic or apyrimidinic site)...
APEX1
41Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There is more potential isoformShow all

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti57G → A in AAA58371 (PubMed:1722334).Curated1
Sequence conflicti306G → A in AAA58371 (PubMed:1722334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS9550.1

Protein sequence database of the Protein Information Resource

More...PIRi		S23550

NCBI Reference Sequences

More...RefSeqi		NP_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

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000216714; ENSP00000216714; ENSG00000100823
ENST00000398030; ENSP00000381111; ENSG00000100823
ENST00000555414; ENSP00000451979; ENSG00000100823

Database of genes from NCBI RefSeq genomes

More...GeneIDi		328

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:328

UCSC genome browser

More...UCSCi		uc058yte.1 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
CCDSiCCDS9550.1
PIRiS23550
RefSeqiNP_001231178.1, NM_001244249.1
NP_001632.2, NM_001641.3
NP_542379.1, NM_080648.2
NP_542380.1, NM_080649.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4QH9X-ray2.18A38-318[»]
4QHDX-ray1.65A38-318[»]
4QHEX-ray1.40A38-318[»]
5CFGX-ray1.80A44-318[»]
5DFFX-ray1.57A/B43-318[»]
5DFHX-ray1.95A/B43-318[»]
5DFIX-ray1.63A/B43-318[»]
5DFJX-ray1.85A/B43-318[»]
5DG0X-ray1.80A/B43-318[»]
5WN0X-ray2.60A/B43-318[»]
5WN1X-ray2.30A/B43-318[»]
5WN2X-ray2.29A/B43-318[»]
5WN3X-ray2.00A/B43-318[»]
5WN4X-ray2.10A/B43-318[»]
5WN5X-ray2.20A/B43-318[»]
6BOQX-ray1.96A/B1-318[»]
6BORX-ray1.84A/B1-318[»]
6BOSX-ray2.30A/B1-318[»]
6BOTX-ray2.30A/B1-318[»]
6BOUX-ray2.54A/B1-318[»]
6BOVX-ray1.98A/B1-318[»]
6BOWX-ray1.59A/B1-318[»]
6MK3X-ray1.48A40-318[»]
6MKKX-ray1.44A40-318[»]
6MKMX-ray1.67A40-318[»]
6MKOX-ray2.09A40-318[»]
SMRiP27695
ModBaseiSearch...

Protein-protein interaction databases

BioGridi106825, 105 interactors
CORUMiP27695
DIPiDIP-6130N
IntActiP27695, 47 interactors
MINTiP27695
STRINGi9606.ENSP00000216714

Chemistry databases

BindingDBiP27695
ChEMBLiCHEMBL5619
DrugBankiDB04967 Lucanthone

DrugCentral

More...DrugCentrali		P27695

PTM databases

iPTMnetiP27695
PhosphoSitePlusiP27695
SwissPalmiP27695

Polymorphism and mutation databases

BioMutaiAPEX1
DMDMi113984

Proteomic databases

CPTACiCPTAC-23
CPTAC-24
EPDiP27695
jPOSTiP27695
MassIVEiP27695
PaxDbiP27695
PeptideAtlasiP27695
PRIDEiP27695
ProteomicsDBi54406
TopDownProteomicsiP27695

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		328
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216714; ENSP00000216714; ENSG00000100823
ENST00000398030; ENSP00000381111; ENSG00000100823
ENST00000555414; ENSP00000451979; ENSG00000100823
GeneIDi328
KEGGihsa:328
UCSCiuc058yte.1 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		328
DisGeNETi328

GeneCards: human genes, protein and diseases

More...GeneCardsi		APEX1
HGNCiHGNC:587 APEX1
HPAiCAB004294
CAB047307
HPA000956
HPA002564
MIMi107748 gene
neXtProtiNX_P27695
OpenTargetsiENSG00000100823
PharmGKBiPA201059

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1294 Eukaryota
COG0708 LUCA
GeneTreeiENSGT00530000063540
HOGENOMiHOG000034586
InParanoidiP27695
KOiK10771
OMAiGTAVFTK
OrthoDBi1105625at2759
PhylomeDBiP27695
TreeFamiTF315048

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)
SIGNORiP27695

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		APEX1 human
EvolutionaryTraceiP27695

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		APEX1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		328

Pharos

More...Pharosi		P27695
PMAP-CutDBiP27695

Protein Ontology

More...PROi		PR:P27695

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000100823 Expressed in 229 organ(s), highest expression level in embryo
ExpressionAtlasiP27695 baseline and differential
GenevisibleiP27695 HS

Family and domain databases

DisProtiDP00007
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAPEX1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P27695
Secondary accession number(s): Q969L5, Q99775
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 236 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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