Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
APE1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
APE1 a multifunctional enzyme that plays a central role in the cellular response to oxidative stress including DNA repair and redox regulation of transcriptional factors. Binds DNA and RNA. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway, a 3'-5' exoribonuclease for mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules, and a DNA 3' phosphodiesterase capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. Is a loading factor for POLB onto non-incised AP sites in DNA, stimulates the 5'-terminal deoxyribose 5'- phosphate (dRp) excision activity of POLB, and involved in the DNA cleavage step of class switch recombination (CSR). Possesses 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. Binds to negative calcium response elements (nCaREs). Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Is an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover. In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. 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. Up-regulated in presence of reactive oxygen species (ROS), like bleomycin, H2O2 and phenazine methosulfate. NPM1 stimulates endodeoxyribonuclease activity on double-stranded DNA with AP sites, but inhibits endoribonuclease activity on single-stranded RNA containing AP sites. Belongs to the DNA repair enzymes AP/ExoA family. Note: This description may include information from UniProtKB.
Protein type: Endoplasmic reticulum; EC 4.2.99.18; Transcription, coactivator/corepressor; Deoxyribonuclease; Lyase; DNA binding protein; EC 3.1.-.-; DNA repair, damage; Hydrolase
Cellular Component: nucleoplasm; centrosome; transcription factor complex; mitochondrion; perinuclear region of cytoplasm; endoplasmic reticulum; cytoplasm; nucleolus; ribosome; nuclear speck; nucleus
Molecular Function: phosphodiesterase I activity; phosphoric diester hydrolase activity; DNA-(apurinic or apyrimidinic site) lyase activity; uracil DNA N-glycosylase activity; chromatin DNA binding; metal ion binding; transcription coactivator activity; oxidoreductase activity; endodeoxyribonuclease activity; NF-kappaB binding; protein binding; DNA binding; endonuclease activity; protein complex binding; damaged DNA binding; ribonuclease H activity; 3'-5' exonuclease activity; transcription corepressor activity; site-specific endodeoxyribonuclease activity, specific for altered base
Biological Process: response to drug; positive regulation of DNA repair; regulation of transcription, DNA-dependent; transcription, DNA-dependent; cell redox homeostasis; base-excision repair; negative regulation of smooth muscle cell migration; regulation of mRNA stability; DNA repair; DNA catabolic process, endonucleolytic; aging; DNA recombination
Reference #:  P27695 (UniProtKB)
Alt. Names/Synonyms: AP endonuclease 1; AP endonuclease class I; AP lyase; APE; APE1; APEN; APEX; APEX nuclease; APEX nuclease (multifunctional DNA repair enzyme) 1; APEX1; Apurinic-apyrimidinic endonuclease 1; apurinic/apyrimidinic (abasic) endonuclease; apurinic/apyrimidinic exonuclease; APX; deoxyribonuclease (apurinic or apyrimidinic); DNA-(apurinic or apyrimidinic site) lyase; HAP1; multifunctional DNA repair enzyme; Protein REF-1; redox factor 1; REF1
Gene Symbols: APEX1
Molecular weight: 35,555 Da
Basal Isoelectric point: 8.33  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

APE1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 K3-a _____MPkRGkkGAV
4 0 K6-a __MPkRGkkGAVAED
4 0 K7-a _MPkRGkkGAVAEDG
0 11 T19 EDGDELRTEPEAkkS
0 3 A23 ELRTEPEAkkSkTAA
0 16 K24-a LRTEPEAkkSkTAAk
1 1 K24-u LRTEPEAkkSkTAAk
1 0 K25-u RTEPEAkkSkTAAkk
0 2 K25-a RTEPEAkkSkTAAkk
2 0 K27-a EPEAkkSkTAAkkND
1 0 K27-u EPEAkkSkTAAkkND
2 0 K31-a kkSkTAAkkNDkEAA
2 0 K32-a kSkTAAkkNDkEAAG
2 2 K35-a TAAkkNDkEAAGEGP
0 9 Y45-p AGEGPALyEDPPDQK
0 1 S54-p DPPDQKTsPSGKPAT
0 1 K125-u YWSAPSDkEGySGVG
0 1 Y128-p APSDkEGySGVGLLS
0 6 Y171-p SFVLVTAyVPNAGRG
0 1 Y184-p RGLVRLEyRQRWDEA
0 1 K197-a EAFRKFLkGLASRKP
0 2 K228-u RNPKGNKkNAGFtPQ
2 0 T233-p NKkNAGFtPQERQGF
0 2 Y262-p HLYPNTPyAYTFWTY
  mouse

 
K3 _____MPKRGKKAAA
K6 __MPKRGKKAAADDG
K7 _MPKRGKKAAADDGE
S18-p DDGEEPKsEPEtKKS
T22-p EPKsEPEtKKSKGAA
K23 PKsEPEtKKSKGAAK
K23 PKsEPEtKKSKGAAK
K24 KsEPEtKKSKGAAKK
K24 KsEPEtKKSKGAAKK
K26 EPEtKKSKGAAKKTE
K26 EPEtKKSKGAAKKTE
K30 KKSKGAAKKTEKEAA
K31 KSKGAAKKTEKEAAG
K34 GAAKKTEKEAAGEGP
Y44 AGEGPVLYEDPPDQK
S53 DPPDQKTSPSGKSAT
K124 YWSAPSDKEGYSGVG
Y127 APSDKEGYSGVGLLS
Y170 SFVLVTAYVPNAGRG
Y183 RGLVRLEYRQRWDEA
K196 EAFRKFLKDLASRKP
K227-u RNPKGNKkNAGFtPQ
T232-p NKkNAGFtPQERQGF
Y261 HLYPNTAYAYTFWTY
  rat

 
K3 _____MPKRGKRAAA
K6 __MPKRGKRAAAEDG
R7 _MPKRGKRAAAEDGE
S18-p EDGEEPKsEPEtKKS
T22-p EPKsEPEtKKSKGAA
K23 PKsEPEtKKSKGAAK
K23 PKsEPEtKKSKGAAK
K24 KsEPEtKKSKGAAKK
K24 KsEPEtKKSKGAAKK
K26 EPEtKKSKGAAKKTE
K26 EPEtKKSKGAAKKTE
K30 KKSKGAAKKTEKEAA
K31 KSKGAAKKTEKEAAG
K34 GAAKKTEKEAAGEGP
Y44 AGEGPVLYEDPPDQK
S53 DPPDQKTSASGKSAT
K124 YWSAPSDKEGYSGVG
Y127 APSDKEGYSGVGLLS
Y170 SFILVTAYVPNAGRG
Y183 RGLVRLEYRQRWDEA
K196 EAFRKFLKDLASRKP
K227 RNPKGNKKNAGFTPQ
T232 NKKNAGFTPQERQGF
Y261 HLYPNTAYAYTFWTY
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.