Difference between revisions of "Sandbox"
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− | * '''Description:''' | + | * '''Description:''' inosine-monophosphate dehydrogenase <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''' | ||
− | |'' | + | |''guaB'' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''guaA '' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes | |style="background:#ABCDEF;" align="center"| '''Essential''' || yes | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || inosine-monophosphate dehydrogenase (EC 1.1.1.205) |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || | + | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 52 kDa, 6.168 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || | + | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1464 bp, 488 aa |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | ||
|- | |- | ||
− | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ | + | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/guaB_nucleotide.txt Gene sequence (+200bp) ]''' |
− | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ | + | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/guaB_protein.txt Protein sequence]''' |
|- | |- | ||
− | |colspan="2" | '''Genetic context''' <br/> [[Image: | + | |colspan="2" | '''Genetic context''' <br/> [[Image:guaB_context.gif]] |
|- | |- | ||
|} | |} | ||
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=== Database entries === | === Database entries === | ||
− | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ | + | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/guaB.html] |
− | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+ | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10073] |
=== Additional information=== | === Additional information=== | ||
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* '''Protein family:''' | * '''Protein family:''' | ||
− | * '''Paralogous protein(s):''' | + | * '''Paralogous protein(s):''' |
=== Extended information on the protein === | === Extended information on the protein === | ||
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* '''Domains:''' | * '''Domains:''' | ||
− | * '''Modification:''' | + | * '''Modification:''' phosphorylated (STY) [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed], S-cysteinlyation after diamide stress (Cys-308) [http://www.ncbi.nlm.nih.gov/pubmed/17611193 PubMed] |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''Interactions:''' |
− | * '''Localization:''' | + | * '''Localization:''' |
=== Database entries === | === Database entries === | ||
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' |
− | * '''Sigma factor:''' | + | * '''Sigma factor:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
− | # | + | # Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in ''Bacillus subtilis''. ''Proteomics'' 7: 3509-3526. [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] |
− | # | + | # Hochgräfe et al. (2007) S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. ''J. Biol. Chem.'' 282: 25981-25985. [http://www.ncbi.nlm.nih.gov/pubmed/17611193 PubMed] |
− |
Revision as of 12:48, 9 February 2009
- Description: inosine-monophosphate dehydrogenase
Gene name | guaB |
Synonyms | guaA |
Essential | yes |
Product | inosine-monophosphate dehydrogenase (EC 1.1.1.205) |
Function | |
MW, pI | 52 kDa, 6.168 |
Gene length, protein length | 1464 bp, 488 aa |
Immediate neighbours | |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
essential
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- 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
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Hochgräfe et al. (2007) S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J. Biol. Chem. 282: 25981-25985. PubMed