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PCNA PCNA MUTYH MUTYH UNG UNG XPA XPA APEX2 APEX2 OGG1 OGG1 ERCC1 ERCC1 ERCC4 ERCC4 APTX APTX PNKP PNKP TDP1 TDP1
"APEX2" - APEX nuclease (apurinic/apyrimidinic endonuclease) 2 in Homo sapiens
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protein of unknown 3D structure
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Predicted Interactions
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APEX2APEX nuclease (apurinic/apyrimidinic endonuclease) 2; Function as a weak 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. Displays also double-stranded DNA 3’-5’ exonuclease, 3’-phosphodiesterase activities. Shows robust 3’-5’ exonuclease activity on 3’-recessed he [...] (518 aa)    
Predicted Functional Partners:
PCNA
proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] (261 aa)
      score_image score_image   score_image   0.996
ERCC4
excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link (916 aa)
      score_image score_image   score_image   0.972
PNKP
polynucleotide kinase 3’-phosphatase; Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3’-phosphates from, or by phosphorylating 5’-hydroxyl groups on, the ribose sugar of the DNA backbone (521 aa)
score_image       score_image   score_image   0.962
APTX
aprataxin (342 aa)
        score_image   score_image   0.960
TDP1
tyrosyl-DNA phosphodiesterase 1; DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3’-phosphodiester bond, giving rise to DNA with a free 3’ phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3’-phosphoglycolates on protruding 3’ ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3’exonuclease activity and can remove a single nucleoside from the [...] (608 aa)
      score_image score_image   score_image   0.951
ERCC1
excision repair cross-complementing rodent repair deficiency, complementation group 1 (includes overlapping antisense sequence); Structure-specific DNA repair endonuclease responsible for the 5’-incision during DNA repair (323 aa)
        score_image   score_image   0.934
XPA
xeroderma pigmentosum, complementation group A; Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (273 aa)
        score_image   score_image   0.910
OGG1
8-oxoguanine DNA glycosylase (424 aa)
        score_image   score_image   0.874
UNG
uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (By similarity) (313 aa)
      score_image score_image   score_image   0.860
MUTYH
mutY homolog (E. coli); Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2- OH-A DNA glycosylase activities (546 aa)
        score_image   score_image   0.858
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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