Rv1642 - 50S ribosomal protein L35 rpmI


Protein Domains

Gene Information
LocusRv1642
SymbolrpmI
Gene Name50S ribosomal protein L35 rpmI
Location1852928 - 1853122 (+)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:195 bp
Protein:65 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number607
Related GenesAcel_1268 BL1366a CE1510 cg1564 DIP1161 jk0835 MAP1353 MAV_3126 Mkms_3024 ML1395 Mmcs_2980 MSMEG_3792 MT1680 MUL_1628 Mvan_3327 nfa19150 PPA1413 SAV6738 SCO1599
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv1642
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,YW. Chow,R. Pietranico,A. Mukerji Studies of oxygen binding energy to hemoglobin molecule. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,N. Choonee,S. Even,L. Zig,H. Putzer Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,F. Allemand,J. Haentjens,C. Chiaruttini,C. Royer,M. Springer Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,YW. Chow,R. Pietranico,A. Mukerji Studies of oxygen binding energy to hemoglobin molecule. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,N. Choonee,S. Even,L. Zig,H. Putzer Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,F. Allemand,J. Haentjens,C. Chiaruttini,C. Royer,M. Springer Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,YW. Chow,R. Pietranico,A. Mukerji Studies of oxygen binding energy to hemoglobin molecule. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,N. Choonee,S. Even,L. Zig,H. Putzer Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Co-expression (Functional linkage)
authors,F. Allemand,J. Haentjens,C. Chiaruttini,C. Royer,M. Springer Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,YW. Chow,R. Pietranico,A. Mukerji Studies of oxygen binding energy to hemoglobin molecule. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,RJ. Smith,RG. Bryant Metal substitutions incarbonic anhydrase: a halide ion probe study. Biochem. Biophys. Res. Commun. 1975
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,N. Choonee,S. Even,L. Zig,H. Putzer Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism. Nucleic Acids Res. 2007
InteractionTranscription Rv1643activesourish102012-10-05
Affinity purification (Physical interaction)
authors,F. Allemand,J. Haentjens,C. Chiaruttini,C. Royer,M. Springer Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 2007