Human N-Glycosylase/DNA Lyase(OOG1) is a DNA repair enzyme, which belongs to the type-1 OGG1 family. OOG1 incises DNA at 8-oxoG residues, and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damage DNA. It has a β-lyase activity that nicks DNA 3’ to the lesion. OOG1 together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. The OGG1 gene mutations may be caused Renal cell carcinoma.

Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells. Uracil-DNA glycosylase exists in two forms: mitochondrial uracil-DNA glycosylase 1 (UNG1) and nuclear uracil-DNA glycosylase 2 (UNG2). uracil-DNA glycosylase. This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2. The UNG2 term was used as a previous symbol for the CCNO gene (GeneID 10309), which has been confused with this gene, in the literature and some databases. Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5). A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.

SMUG1 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 35.6 kDa and the accession number is Q53HV7.

DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion. OGG1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 42.8 kDa and the accession number is O15527.

E3 ubiquitin ligase required to protect genome stability in response to replication stress. Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription. Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex. Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3. If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway. Only catalyzes ubiquitination of MCM7 when forks converge. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome. Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity. The function in translesion synthesis is however controversial. Acts as a regulator of the spindle assembly checkpoint. Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation.

Apurinic-Apyrimidinic Endonuclease 1 (APE1) is required for efficient DNA base excision repair. When the DNA glycosylase remove the damaged bases, APE1 cleaves the AP site to allow resynthesis and ligation to complete repair. APE1 stimulates the DNA binding activity of many transcription factors, which participate in cancer promotion and progression. APE1 regulates the redox state of multiple transcription factors, such as c-Jun, c-Fos, NF-kB, p53. APEN is also involved in calcium-dependent down-regulation of PTH expression.

NEIL1 is a member of DNA glycosylases. DNA glycosylases are a family homologous to the bacterial Fpg/Nei family. They play a role in base excision repair which is the mechanism by which damaged bases in DNA are removed and replaced. The first step of this process is catalyzed by DNA glycosylases. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. NEIL1 functions in base excision repair of DNA damaged by oxidation or by mutagenic agents. It acts as a DNA glycosylase that recognizes and removes damaged bases. NEIL1 prefers to oxidized pyrimidines, such as thymine glycol, Formamidopyrimidine (Fapy), and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. It has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand and cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.