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APEX1:AP-dsDNAAPEX1:SSB(AP->5'-dRP)-dsDNAAPEX1:SSB(5'-ddRP)-dsDNAPOLB:APEX1:SSB(3'dNMP-displaced 5'ddRP)-dsDNAAPEX1:FEN1:PCNA:POLD;POLE:RPA:RFC:SSB(3'dNMP-displaced 5'ddRP)-dsDNAAPEX1:FEN1:PCNA:POLD;POLE:RPA:RFC:SSB(3'poly-dNMP-displaced 5'ddRP flap)-dsDNAAPEX1:PCNA:POLD;POLE:RPA:RFC:SSB(3'poly-dNMP)-dsDNALIG1:APEX1:PCNA:POLD;POLE:RPA:RFC:dsDNADisplacement of UNG glycosylase by APEX1 at the AP siteDisplacement of TDG glycosylase by APEX1 at the AP siteDisplacement of SMUG1 glycosylase by APEX1 at the AP siteDisplacement of NTHL1 glycosylase by APEX1 at the AP siteDisplacement of MBD4 glycosylase by APEX1 at the AP siteDisplacement of OGG1 glycosylase by APEX1 at the AP siteDisplacement of MUTYH glycosylase by APEX1 at the AP siteDisplacement of MPG glycosylase by APEX1 at the AP siteExcision of the abasic sugar phosphate (5'dRP) residue at the single strand breakPARP1;PARP2 dimers and FEN1 bind POLB and displace APEX1 from damaged AP siteLIG1; APEX1 and PCNA:POLD;POLE:RPA:RFC dissociate from repaired DNA
P527
P688
Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effectsTwo divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanismSequence analysis identifies TTRAP, a protein that associates with CD40 and TNF receptor-associated factors, as a member of a superfamily of divalent cation-dependent phosphodiesterasesHuman AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoterAn exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3' mispaired DNACharacterization of a wide range base-damage-endonuclease activity of mammalian rpS3Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brainIdentification and characterization of mitochondrial targeting sequence of human apurinic/apyrimidinic endonuclease 1Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonanceAnalysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1).Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicalsHuman ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activityIdentification of redox/repair protein Ref-1 as a potent activator of p53Identification of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNASIRT1 deacetylates APE1 and regulates cellular base excision repairUVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear specklesAPE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process.A redox factor protein, ref1, is involved in negative gene regulation by extracellular calciumCleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme AAPE1 incision activity at abasic sites in tandem repeat sequencesDrosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activityNuclear complex of glyceraldehyde-3-phosphate dehydrogenase and DNA repair enzyme apurinic/apyrimidinic endonuclease I protect smooth muscle cells against oxidant-induced cell death.
P921
Q50253148-EAB57FE3-BE57-4603-ADE1-23ACB2FE7066Q50253152-42CBE486-216B-4B63-AC40-4A5D5A362470Q50253180-D57967E8-A1F5-4587-AF03-846810BA6B36Q50253184-DB3335BD-FC6A-4DB8-912E-9055634796E8Q50253208-8DF501A3-CAB5-4251-A043-3FBFA4A2A99FQ50253210-302D30CD-74B2-43D3-9D41-D94E76867D7BQ50253213-6FC9EFC3-0EEB-4C17-A3B3-B982B091EAC5Q50253217-FA82CC3B-771F-4F67-86DC-5530EFDC17B1Q50287199-4DB5516F-96A7-4385-89B8-FBCAD96CA88AQ50287200-866B9156-DE05-4AB9-ACD8-52341B90BF24Q50287202-4159ED94-171D-40AC-A499-2046C34CDF2CQ50287203-B2097F0B-1173-4CED-9766-C88A9F99FF15Q50287204-3751213D-EBC3-4776-94C4-22C5665B1598Q50287205-CEBB8AD9-1EFE-4725-A836-503987038E9DQ50287207-4DB413F7-D122-470C-AD4B-D897B5C3553AQ50287208-ACAFAF59-4993-4302-8B1C-745E1CCCC214Q50287211-4E2FF1CA-ACC7-409D-AA71-14DBBBF381B2Q50287231-939FC9AF-B4EF-490A-9339-0C502C090246Q50287247-3F729DC9-3467-41FC-9980-4D5B917E7C03
P527
Q22254069-345CF859-0D8D-4210-AA1E-AC427E022BA4Q24291085-E23E7EA6-91C1-45D1-A94D-4DE52A2D554AQ24291496-7C719141-3194-4858-80BD-5A207FF9773AQ24292228-CE9DA1BA-67FC-408D-B643-9759A457207CQ24292267-7AF0471A-0B85-4BE4-9CEF-00230177AB55Q24294834-4B5E367A-DE81-4280-9B8E-7DFE87195D7CQ24299862-BF4B791F-3C24-463B-8B1E-6AF4E65E0CBAQ24303442-729A8225-4975-4BD3-A395-F82AE7CB34F9Q24303949-2C74390E-01A9-4D65-8E99-5EF2D12765BAQ24304919-BB22C6FE-677C-4035-8C0A-1FAB2C9B95E9Q24310136-E2F7FCBC-7C4A-4577-A060-51A57128A836Q24310335-27A8AD74-66CA-4CF5-BF49-CBEC900F7709Q24316161-57DF3D35-A749-4465-89FA-C29510ED8232Q24319977-C0E7A45D-E565-47D1-AD03-B107408BBAA5Q24320136-16A7652B-1765-4A9C-962E-E9FFDE1F861FQ24323047-A3D72ACB-6DC2-4E3F-BF77-DDD72D04C622Q24329154-7437D41D-B30E-44A7-9F1A-E3AD8C50C29BQ24337016-88EAEB9C-F4BA-4A10-B363-52107D15C549Q24338600-D81F81FA-9360-4BF0-95AC-ABDFEACBDF10Q28118887-80C381BB-6C31-4038-ABE5-4277003A8655Q28910449-4B76A91C-B104-414D-89D1-FCFCB8DEF816Q51061720-C5D02654-A742-4008-A1F9-4AC1E2CA69EA
P921
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
proteïne in Apurinic/apyrimidinic endodeoxyribonuclease 1
@nl
protèin
@ace
بروتين في الإنسان العاقل
@ar
name
Apurinic/apyrimidinic endodeoxyribonuclease 1
@en
Apurinic/apyrimidinic endodeoxyribonuclease 1
@nl
type
label
Apurinic/apyrimidinic endodeoxyribonuclease 1
@en
Apurinic/apyrimidinic endodeoxyribonuclease 1
@nl
altLabel
AP endonuclease 1
@en
AP endonuclease class I
@en
AP lyase
@en
APE-1
@en
APEN
@en
APEX nuclease (multifunctional DNA repair enzyme) 1
@en
APEX nuclease
@en
APEX1
@en
DNA-(apurinic or apyrimidinic site) lyase
@en
REF-1
@en
prefLabel
Apurinic/apyrimidinic endodeoxyribonuclease 1
@en
Apurinic/apyrimidinic endodeoxyribonuclease 1
@nl
P527
P637
P638
P680
P681
P682
P705
P352
P279
P31
P352
P527
P637
NP_001231178
P638
P680
P681
P682
P702
P703
P705
ENSP00000216714
ENSP00000381111
ENSP00000416414
ENSP00000450604
ENSP00000451060
ENSP00000451170
ENSP00000451327
ENSP00000451491
ENSP00000451979
ENSP00000452137