Difference between revisions of "Aag"
 (New page: * '''Description:''' write here <br/><br/>  {| align="right" border="1" cellpadding="2"  |- |style="background:#ABCDEF;" align="center"|'''Gene name''' |''yxlJ'' |- |style="background:#ABC...)  | 
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| Line 1: | Line 1: | ||
| − | * '''Description:'''   | + | * '''Description:''' 3-methyladenine DNA glycosylase <br/><br/>  | 
{| align="right" border="1" cellpadding="2"    | {| align="right" border="1" cellpadding="2"    | ||
|-  | |-  | ||
|style="background:#ABCDEF;" align="center"|'''Gene name'''  | |style="background:#ABCDEF;" align="center"|'''Gene name'''  | ||
| − | |''  | + | |''aag''  | 
|-  | |-  | ||
| − | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''  | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yxlJ ''  | 
|-  | |-  | ||
| − | |style="background:#ABCDEF;" align="center"| '''Essential''' ||    | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || no  | 
|-  | |-  | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' ||    | + | |style="background:#ABCDEF;" align="center"| '''Product''' || 3-methyladenine DNA glycosylase  | 
|-  | |-  | ||
| − | |style="background:#ABCDEF;" align="center"|'''Function''' ||   | + | |style="background:#ABCDEF;" align="center"|'''Function''' || DNA repair  | 
|-  | |-  | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 6.117     | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 6.117     | ||
| Line 52: | Line 52: | ||
=== Basic information/ Evolution ===  | === Basic information/ Evolution ===  | ||
| − | * '''Catalyzed reaction/ biological activity:'''    | + | * '''Catalyzed reaction/ biological activity:''' removes hypoxanthine, 3-alkylated purines, and 1,N6-ethenoadenine from DNA; hypoxanthine and 1,N6-ethenoadenine are the preferred substrates  | 
| − | * '''Protein family:'''  | + | * '''Protein family:''' AAG family of 3-methyladenine DNA glycosylases  | 
* '''Paralogous protein(s):'''  | * '''Paralogous protein(s):'''  | ||
| Line 118: | Line 118: | ||
=References=  | =References=  | ||
| − | #   | + | # Aamodt et al. (2004) The ''Bacillus subtilis'' counterpart of the mammalian 3-methyladenine DNA glycosylase has hypoxanthine and 1,N6-ethenoadenine as preferred substrates. ''J. Biol. Chem.'' '''279:''' 13601-13606-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/14729667 PubMed]  | 
Revision as of 13:59, 13 February 2009
-  Description: 3-methyladenine DNA glycosylase 
 
| Gene name | aag | 
| Synonyms | yxlJ | 
| Essential | no | 
| Product | 3-methyladenine DNA glycosylase | 
| Function | DNA repair | 
| MW, pI | 21 kDa, 6.117 | 
| Gene length, protein length | 588 bp, 196 aa | 
| Immediate neighbours | |
| Gene sequence (+200bp) | Protein sequence | 
 Genetic context  
 | |
Contents
The gene
Basic information
- Coordinates:
 
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
 
- SubtiList entry: [2]
 
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: removes hypoxanthine, 3-alkylated purines, and 1,N6-ethenoadenine from DNA; hypoxanthine and 1,N6-ethenoadenine are the preferred substrates
 
- Protein family: AAG family of 3-methyladenine DNA glycosylases
 
- Paralogous protein(s):
 
Extended information on the protein
- Kinetic information:
 
- Domains:
 
- Modification:
 
- Cofactor(s):
 
- Effectors of protein activity:
 
- Interactions:
 
- Localization:
 
Database entries
- Structure:
 
- Swiss prot entry:
 
- KEGG entry:
 
- E.C. number:
 
Additional information
Expression and regulation
- Operon:
 
- Sigma factor:
 
- Regulation:
 
- Regulatory mechanism:
 
- Additional information:
 
Biological materials
- Mutant:
 
- Expression vector:
 
- lacZ fusion:
 
- GFP fusion:
 
- two-hybrid system:
 
- Antibody:
 
Labs working on this gene/protein
Your additional remarks
References
- Aamodt et al. (2004) The Bacillus subtilis counterpart of the mammalian 3-methyladenine DNA glycosylase has hypoxanthine and 1,N6-ethenoadenine as preferred substrates. J. Biol. Chem. 279: 13601-13606-page. PubMed
 
