HUMAN:APEX1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	APEX1 (synonyms: APE, APE1, APEX, APX, HAP1, REF1)
Protein Name(s)	DNA-(apurinic or apyrimidinic site) lyase APEX nuclease APEN Apurinic-apyrimidinic endonuclease 1 AP endonuclease 1 APE-1 REF-1 Redox factor-1 DNA-(apurinic or apyrimidinic site) lyase, mitochondrial
External Links
UniProt	P27695
EMBL	X59764 M80261 D90373 S43127 M81955 M92444 X66133 D13370 U79268 BT007236 AF488551 AL355075 BC002338 BC004979 BC008145 BC019291 M99703
CCDS	CCDS9550.1
PIR	S23550
RefSeq	NP_001231178.1 NP_001632.2 NP_542379.1 NP_542380.1 XP_005267638.1
UniGene	Hs.73722
PDB	1BIX 1CQG 1CQH 1DE8 1DE9 1DEW 1E9N 1HD7 2ISI 2O3H 3U8U 4IEM 4LND 4QH9 4QHD 4QHE 5DFF 5DFH 5DFI 5DFJ 5DG0
PDBsum	1BIX 1CQG 1CQH 1DE8 1DE9 1DEW 1E9N 1HD7 2ISI 2O3H 3U8U 4IEM 4LND 4QH9 4QHD 4QHE 5DFF 5DFH 5DFI 5DFJ 5DG0
DisProt	DP00007
ProteinModelPortal	P27695
SMR	P27695
BioGrid	106825
DIP	DIP-6130N
IntAct	P27695
MINT	MINT-119189
STRING	9606.ENSP00000216714
BindingDB	P27695
ChEMBL	CHEMBL5619
DrugBank	DB04967
iPTMnet	P27695
PhosphoSite	P27695
SwissPalm	P27695
BioMuta	APEX1
DMDM	113984
EPD	P27695
PaxDb	P27695
PeptideAtlas	P27695
PRIDE	P27695
TopDownProteomics	P27695
DNASU	328
Ensembl	ENST00000216714 ENST00000398030 ENST00000555414
GeneID	328
KEGG	hsa:328
UCSC	uc058yte.1
CTD	328
GeneCards	APEX1
HGNC	HGNC:587
HPA	CAB004294 CAB047307 HPA000956 HPA002564
MIM	107748
neXtProt	NX_P27695
PharmGKB	PA201059
eggNOG	KOG1294 COG0708
HOGENOM	HOG000034586
HOVERGEN	HBG050531
InParanoid	P27695
KO	K10771
OMA	YTPNSQQ
OrthoDB	EOG7C8GJ6
PhylomeDB	P27695
TreeFam	TF315048
BRENDA	4.2.99.18
Reactome	R-HSA-110357 R-HSA-110362 R-HSA-110373 R-HSA-174414 R-HSA-5651801 R-HSA-69183 R-HSA-73930 R-HSA-73933
ChiTaRS	APEX1
EvolutionaryTrace	P27695
GeneWiki	APEX1
GenomeRNAi	328
NextBio	1347
PMAP-CutDB	P27695
PRO	PR:P27695
Proteomes	UP000005640
Bgee	P27695
CleanEx	HS_APEX1 HS_HAP1
ExpressionAtlas	P27695
Genevisible	P27695
GO	GO:0005813 GO:0005737 GO:0005783 GO:0005739 GO:0000784 GO:0016607 GO:0005730 GO:0005654 GO:0005634 GO:0048471 GO:0005840 GO:0005667 GO:0008408 GO:0031490 GO:0003684 GO:0003677 GO:0003906 GO:0008311 GO:0008309 GO:0003691 GO:0004520 GO:0004519 GO:0046872 GO:0016491 GO:0004528 GO:0008081 GO:0044822 GO:0004523 GO:0016890 GO:0003713 GO:0003714 GO:0004844 GO:0007568 GO:0006284 GO:0045454 GO:0071320 GO:0070301 GO:0071375 GO:0080111 GO:0006281 GO:0006271 GO:0000278 GO:1903507 GO:0014912 GO:0055114 GO:0045739 GO:1900087 GO:0043488 GO:0006355 GO:0042493 GO:0000723 GO:0000722 GO:0032201 GO:0006351
Gene3D	3.60.10.10
InterPro	IPR004808 IPR020847 IPR020848 IPR005135
PANTHER	PTHR22748
Pfam	PF03372
SUPFAM	SSF56219
TIGRFAMs	TIGR00633
PROSITE	PS00726 PS00727 PS00728 PS51435

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005634	nucleus	PMID:28404743^[1]	ECO:0000314			C		HUMAN APEX1 (Ape1) // “In control and H2O2-treated cells, immunoreactive Ape1 was localized in the nucleus,” (Fig 3C-D).	complete CACAO 12695
	GO:0005737	cytoplasm	PMID:28404743^[1]	ECO:0000314			C		HUMAN APEX1 (Ape1) // “GAPDH and Ape1 localization in the cytoplasmic and nuclear compartments of SMCs after a short-term exposure to H2O2 (110mM for 6 h) was visualized by conventional confocal microscopy (Fig. 3C)."	complete CACAO 12696
	GO:0016893	endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters	PMID:28404743^[1]	ECO:0000315			F		HUMAN APEX1 (Ape1) // From figure description: “The 5’-endonuclease activity of Ape1 was quantified by measuring the incision of a 26-mer FAM-labeled oligonucleotide substrate that contained a single synthetic AP site,” (Fig. 5C,D). Ape1 nuclear activity was increased in R3 cells when compared to WT cells.	complete CACAO 12697
	GO:0004519	endonuclease activity	PMID:28404743^[1]	ECO:0000315			F		HUMAN APEX1 (Ape1) // From figure description: “The 5’-endonuclease activity of Ape1 was quantified by measuring the incision of a 26-mer FAM-labeled oligonucleotide substrate that contained a single synthetic AP site,” (Fig. 5C,D). Ape1 nuclear activity was increased in R3 cells when compared to WT cells.	complete CACAO 12698
	GO:0003697	single-stranded DNA binding	PMID:26773055^[2]	ECO:0000314			F		in Figure 3A, histogram displaying a ChIP analysis assessing Sp1 binding to APEX1 proximal promoter. The assay was carried out using TIG-1 cells transfected with either a control siRNA, a XRCC1 siRNA or a Sp1-targeting siRNA (as positive control for signal reduction). Results are expressed as mean fold enrichment over unspecific IgG relative to control siRNA ± SD of three independent experiments.	complete CACAO 12775
involved_in	GO:0006284	base-excision repair	PMID:8932386^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:8932386^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008081	phosphoric diester hydrolase activity	PMID:18973764^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:18973764^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:15707971^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:24703901^[6]	ECO:0000305	curator inference used in manual assertion	GO:0000723 GO:0003691	C		Seeded From UniProt	complete
enables	GO:0008309	double-stranded DNA exodeoxyribonuclease activity	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0000723)	Seeded From UniProt	complete
enables	GO:0016890	site-specific endodeoxyribonuclease activity, specific for altered base	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0000723)	Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0000723)	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0000723)	Seeded From UniProt	complete
involved_in	GO:0097698	telomere maintenance via base-excision repair	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:24703901^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:14706345^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0080111	DNA demethylation	PMID:21496894^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:12524539^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	PMID:11286553^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	PMID:19934257^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043488	regulation of mRNA stability	PMID:19401441^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031490	chromatin DNA binding	PMID:11809897^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016890	site-specific endodeoxyribonuclease activity, specific for altered base	PMID:19188445^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	PMID:17148573^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:12524539^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:9119221^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:11832948^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:9560228^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20231292^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9560228^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:17148573^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:19188445^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:17148573^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15942031^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:19934257^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9119221^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:19188445^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:9119221^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:12524539^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:11286553^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008311	double-stranded DNA 3'-5' exodeoxyribonuclease activity	PMID:21873635^[22]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000507731 PomBase:SPBC3D6.10 SGD:S000000115	F		Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:21873635^[22]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000507731 SGD:S000000115 UniProtKB:P27695 WB:WBGene00001372	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[22]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1924872 MGI:MGI:88042 PANTHER:PTN000507732 PomBase:SPBC3D6.10 RGD:2126 UniProtKB:P27695 UniProtKB:Q9UBZ4	C		Seeded From UniProt	complete
enables	GO:0004528	phosphodiesterase I activity	PMID:21873635^[22]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000507731 PomBase:SPBC3D6.10 UniProtKB:P45951	F		Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:21873635^[22]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004584 PANTHER:PTN000507731 PomBase:SPBC3D6.10 SGD:S000000115 UniProtKB:P27695 UniProtKB:P45951 WB:WBGene00001372	F		Seeded From UniProt	complete
enables	GO:0008081	phosphoric diester hydrolase activity	PMID:11478795^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:11478795^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0016491	P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0016491	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004519	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008408	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004528	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004519	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008408	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008311	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004528	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004519	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004527	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P		Seeded From UniProt	complete
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004521	P		Seeded From UniProt	complete
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004523	P		Seeded From UniProt	complete
involved_in	GO:1903507	negative regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003714	P		Seeded From UniProt	complete
involved_in	GO:1903508	positive regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003713	P		Seeded From UniProt	complete
involved_in	GO:0045454	cell redox homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28352 ensembl:ENSMUSP00000042602	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28352 ensembl:ENSMUSP00000042602	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28352 ensembl:ENSMUSP00000042602	C		Seeded From UniProt	complete
involved_in	GO:1900087	positive regulation of G1/S transition of mitotic cell cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0071417	cellular response to organonitrogen compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0071375	cellular response to peptide hormone stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0071320	cellular response to cAMP	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0070301	cellular response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
enables	GO:0051059	NF-kappaB binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	F		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	F		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0014912	negative regulation of smooth muscle cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0010243	response to organonitrogen compound	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	C		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	C		Seeded From UniProt	complete
enables	GO:0004521	endoribonuclease activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P43138 ensembl:ENSRNOP00000068673	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020847 InterPro:IPR020848	F		Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004808	F		Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020847 InterPro:IPR020848	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004808 InterPro:IPR020847 InterPro:IPR020848	P		Seeded From UniProt	complete
enables	GO:0140078	class I DNA-(apurinic or apyrimidinic site) endonuclease activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.99.18	F		Seeded From UniProt	complete
enables	GO:0004844	uracil DNA N-glycosylase activity	PMID:10805771^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004520	endodeoxyribonuclease activity	PMID:1722334^[25] Reactome:R-HSA-110359	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:7961715^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:11286553^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005840	ribosome	PMID:12524539^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:12524539^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004528	phosphodiesterase I activity	PMID:9119221^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004523	RNA-DNA hybrid ribonuclease activity	PMID:11286553^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:9119221^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006286	base-excision repair, base-free sugar-phosphate removal	Reactome:R-HSA-110375	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	Reactome:R-HSA-73884	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-5651809 Reactome:R-HSA-5651805 Reactome:R-HSA-5649873 Reactome:R-HSA-5649856 Reactome:R-HSA-5649854 Reactome:R-HSA-111253 Reactome:R-HSA-110375 Reactome:R-HSA-110371 Reactome:R-HSA-110368 Reactome:R-HSA-110364 Reactome:R-HSA-110363 Reactome:R-HSA-110360 Reactome:R-HSA-110359 Reactome:R-HSA-110356 Reactome:R-HSA-110355 Reactome:R-HSA-110354 Reactome:R-HSA-110353 Reactome:R-HSA-110352 Reactome:R-HSA-110351 Reactome:R-HSA-110350 Reactome:R-HSA-110349	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0269	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0233	P		Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0186	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Hou, X et al. (2017) Nuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death. FASEB J. PubMed GONUTS page
↑ Poletto, M et al. (2016) p53 coordinates base excision repair to prevent genomic instability. Nucleic Acids Res. 44 3165-75 PubMed GONUTS page
↑ ^3.0 ^3.1 Yacoub, A et al. (1996) Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity. Nucleic Acids Res. 24 4298-303 PubMed GONUTS page
↑ ^4.0 ^4.1 Ko, SI et al. (2008) Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity. Mutat. Res. 648 54-64 PubMed GONUTS page
↑ Kim, SH et al. (2005) Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3. Biochem. Biophys. Res. Commun. 328 962-7 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 ^6.7 Li, M et al. (2014) APE1 incision activity at abasic sites in tandem repeat sequences. J. Mol. Biol. 426 2183-98 PubMed GONUTS page
↑ Hegde, V et al. (2004) Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance. DNA Repair (Amst.) 3 121-6 PubMed GONUTS page
↑ Guo, JU et al. (2011) Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain. Cell 145 423-34 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 Fan, Z et al. (2003) Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A. Nat. Immunol. 4 145-53 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Beernink, PT et al. (2001) 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 1023-34 PubMed GONUTS page
↑ ^11.0 ^11.1 Yamamori, T et al. (2010) SIRT1 deacetylates APE1 and regulates cellular base excision repair. Nucleic Acids Res. 38 832-45 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Barnes, T et al. (2009) Identification of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA. Nucleic Acids Res. 37 3946-58 PubMed GONUTS page
↑ Kuninger, DT et al. (2002) Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter. Nucleic Acids Res. 30 823-9 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Vascotto, C et al. (2009) APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process. Mol. Cell. Biol. 29 1834-54 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Campalans, A et al. (2007) UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles. J. Cell. Sci. 120 23-32 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 Jayaraman, L et al. (1997) Identification of redox/repair protein Ref-1 as a potent activator of p53. Genes Dev. 11 558-70 PubMed GONUTS page
↑ Chou, KM & Cheng, YC (2002) An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3' mispaired DNA. Nature 415 655-9 PubMed GONUTS page
↑ ^19.0 ^19.1 Ramana, CV et al. (1998) 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 5061-6 PubMed GONUTS page
↑ Li, M et al. (2010) Identification and characterization of mitochondrial targeting sequence of human apurinic/apyrimidinic endonuclease 1. J. Biol. Chem. 285 14871-81 PubMed GONUTS page
↑ Jackson, EB et al. (2005) Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1). Nucleic Acids Res. 33 3303-12 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 ^22.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^23.0 ^23.1 Rodrigues-Lima, F et al. (2001) Sequence analysis identifies TTRAP, a protein that associates with CD40 and TNF receptor-associated factors, as a member of a superfamily of divalent cation-dependent phosphodiesterases. Biochem. Biophys. Res. Commun. 285 1274-9 PubMed GONUTS page
↑ Parikh, SS et al. (2000) Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects. Proc. Natl. Acad. Sci. U.S.A. 97 5083-8 PubMed GONUTS page
↑ Demple, B et al. (1991) 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 11450-4 PubMed GONUTS page
↑ Okazaki, T et al. (1994) A redox factor protein, ref1, is involved in negative gene regulation by extracellular calcium. J. Biol. Chem. 269 27855-62 PubMed GONUTS page

[PMID:28404743-1] 1.0 ^1.1 ^1.2 ^1.3 Hou, X et al. (2017) Nuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death. FASEB J. PubMed GONUTS page

[PMID:26773055-2] Poletto, M et al. (2016) p53 coordinates base excision repair to prevent genomic instability. Nucleic Acids Res. 44 3165-75 PubMed GONUTS page

[PMID:8932386-3] 3.0 ^3.1 Yacoub, A et al. (1996) Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity. Nucleic Acids Res. 24 4298-303 PubMed GONUTS page

[PMID:18973764-4] 4.0 ^4.1 Ko, SI et al. (2008) Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity. Mutat. Res. 648 54-64 PubMed GONUTS page

[PMID:15707971-5] Kim, SH et al. (2005) Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3. Biochem. Biophys. Res. Commun. 328 962-7 PubMed GONUTS page

[PMID:24703901-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 ^6.7 Li, M et al. (2014) APE1 incision activity at abasic sites in tandem repeat sequences. J. Mol. Biol. 426 2183-98 PubMed GONUTS page

[PMID:14706345-7] Hegde, V et al. (2004) Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance. DNA Repair (Amst.) 3 121-6 PubMed GONUTS page

[PMID:21496894-8] Guo, JU et al. (2011) Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain. Cell 145 423-34 PubMed GONUTS page

[PMID:12524539-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 Fan, Z et al. (2003) Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A. Nat. Immunol. 4 145-53 PubMed GONUTS page

[PMID:11286553-10] 10.0 ^10.1 ^10.2 ^10.3 Beernink, PT et al. (2001) 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 1023-34 PubMed GONUTS page

[PMID:19934257-11] 11.0 ^11.1 Yamamori, T et al. (2010) SIRT1 deacetylates APE1 and regulates cellular base excision repair. Nucleic Acids Res. 38 832-45 PubMed GONUTS page

[PMID:22681889-12] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:19401441-13] Barnes, T et al. (2009) Identification of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA. Nucleic Acids Res. 37 3946-58 PubMed GONUTS page

[PMID:11809897-14] Kuninger, DT et al. (2002) Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter. Nucleic Acids Res. 30 823-9 PubMed GONUTS page

[PMID:19188445-15] 15.0 ^15.1 ^15.2 Vascotto, C et al. (2009) APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process. Mol. Cell. Biol. 29 1834-54 PubMed GONUTS page

[PMID:17148573-16] 16.0 ^16.1 ^16.2 Campalans, A et al. (2007) UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles. J. Cell. Sci. 120 23-32 PubMed GONUTS page

[PMID:9119221-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 Jayaraman, L et al. (1997) Identification of redox/repair protein Ref-1 as a potent activator of p53. Genes Dev. 11 558-70 PubMed GONUTS page

[PMID:11832948-18] Chou, KM & Cheng, YC (2002) An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3' mispaired DNA. Nature 415 655-9 PubMed GONUTS page

[PMID:9560228-19] 19.0 ^19.1 Ramana, CV et al. (1998) 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 5061-6 PubMed GONUTS page

[PMID:20231292-20] Li, M et al. (2010) Identification and characterization of mitochondrial targeting sequence of human apurinic/apyrimidinic endonuclease 1. J. Biol. Chem. 285 14871-81 PubMed GONUTS page

[PMID:15942031-21] Jackson, EB et al. (2005) Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1). Nucleic Acids Res. 33 3303-12 PubMed GONUTS page

[PMID:21873635-22] 22.0 ^22.1 ^22.2 ^22.3 ^22.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:11478795-23] 23.0 ^23.1 Rodrigues-Lima, F et al. (2001) Sequence analysis identifies TTRAP, a protein that associates with CD40 and TNF receptor-associated factors, as a member of a superfamily of divalent cation-dependent phosphodiesterases. Biochem. Biophys. Res. Commun. 285 1274-9 PubMed GONUTS page

[PMID:10805771-24] Parikh, SS et al. (2000) Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects. Proc. Natl. Acad. Sci. U.S.A. 97 5083-8 PubMed GONUTS page

[PMID:1722334-25] Demple, B et al. (1991) 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 11450-4 PubMed GONUTS page

[PMID:7961715-26] Okazaki, T et al. (1994) A redox factor protein, ref1, is involved in negative gene regulation by extracellular calcium. J. Biol. Chem. 269 27855-62 PubMed GONUTS page

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HUMAN:APEX1

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