RegulonDB RegulonDB 10.10: Gene Form
   

rplE gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

rplE rplX rpsN TSS_3774 (cluster) TSS_3774 (cluster) TSS_3773 TSS_3773 TSS_3772 TSS_3772 TSS_3771 (cluster) TSS_3771 (cluster) TSS_3770 TSS_3770 TSS_3769 TSS_3769 TSS_3768 (cluster) TSS_3768 (cluster) TSS_3767 (cluster) TSS_3767 (cluster) TSS_3766 TSS_3766 TSS_3765 TSS_3765 TSS_3764 TSS_3764 TSS_3763 TSS_3763 TSS_3762 (cluster) TSS_3762 (cluster) TSS_3761 (cluster) TSS_3761 (cluster) TSS_3760 (cluster) TSS_3760 (cluster) TSS_3759 (cluster) TSS_3759 (cluster) TSS_3758 TSS_3758 TSS_3757 TSS_3757 TSS_3756 TSS_3756 TSS_3755 (cluster) TSS_3755 (cluster) TSS_3754 (cluster) TSS_3754 (cluster) TSS_3753 TSS_3753 TSS_3752 TSS_3752

Gene      
Name: rplE    Texpresso search in the literature
Synonym(s): ECK3295, EG10868, b3308
Genome position(nucleotides): 3446899 <-- 3447438 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
49.81
External database links:  
ASAP:
ABE-0010833
CGSC:
259
ECHOBASE:
EB0861
ECOLIHUB:
rplE
MIM:
612562
OU-MICROARRAY:
b3308
STRING:
511145.b3308
COLOMBOS: rplE


Product      
Name: 50S ribosomal subunit protein L5
Synonym(s): RplE
Sequence: Get amino acid sequence Fasta Format
Cellular location: ribosome,cytosol
Molecular weight: 20.302
Isoelectric point: 10.028
Motif(s):
 
Type Positions Sequence
2 -> 179 AKLHDYYKDEVVKKLMTEFNYNSVMQVPRVEKITLNMGVGEAIADKKLLDNAAADLAAISGQKPLITKARKSVAGFKIRQGYPIGCKVTLRGERMWEFFERLITIAVPRIRDFRGLSAKSFDGRGNYSMGVREQIIFPEIDYDKVDRVRGLDITITTTAKSDEEGRALLAAFDFPFRK
24 -> 80 SVMQVPRVEKITLNMGVGEAIADKKLLDNAAADLAAISGQKPLITKARKSVAGFKIR
127 -> 127 N
94 -> 94 E
84 -> 177 PIGCKVTLRGERMWEFFERLITIAVPRIRDFRGLSAKSFDGRGNYSMGVREQIIFPEIDYDKVDRVRGLDITITTTAKSDEEGRALLAAFDFPF

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.2 - translation
  2 - information transfer --> 2.3 - protein related --> 2.3.8 - ribosomal proteins
  6 - cell structure --> 6.6 - ribosomes
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0005840 - ribosome
GO:0022625 - cytosolic large ribosomal subunit
molecular_function GO:0003735 - structural constituent of ribosome
GO:0003723 - RNA binding
GO:0000049 - tRNA binding
GO:0019843 - rRNA binding
GO:0008097 - 5S rRNA binding
biological_process GO:0006412 - translation
GO:0000027 - ribosomal large subunit assembly
Note(s): Note(s): ...[more].
Reference(s): [1] Abdurashidova GG., et al., 1991
[2] Agrawal RK., et al., 2004
[3] Andrieux E., et al., 1984
[4] Bernabeu C., et al., 1976
[5] Branlant C., et al., 1977
[6] Cerretti DP., et al., 1983
[7] Chang CN., et al., 1975
[8] Chang FN., et al., 1974
[9] Chen R., et al., 1976
[10] Dabbs ER. 1977
[11] Dey D., et al., 1998
[12] Dontsova OA., et al., 1990
[13] Fox JW., et al., 1978
[14] Gao H., et al., 2003
[15] Garrett RA., et al., 1979
[16] Goringer HU., et al., 1986
[17] Herfurth E., et al., 1995
[18] Herold M., et al., 1987
[19] Isono K., et al., 1977
[20] Jaskunas SR., et al., 1977
[21] Jaskunas SR., et al., 1977
[22] Kakegawa T., et al., 1986
[23] Kashiwagi K., et al., 1987
[24] Kenny JW., et al., 1975
[25] Larrinua I., et al., 1979
[26] Lotti M., et al., 1989
[27] Maimets TO., et al., 1981
[28] Maly P., et al., 1983
[29] Meng J., et al., 2012
[30] Metspalu E., et al., 1982
[31] Morrison CA., et al., 1977
[32] Nag B., et al., 1987
[33] Newberry V., et al., 1980
[34] Osswald M., et al., 1990
[35] Randolph-Anderson BL., et al., 1989
[36] Redl B., et al., 1989
[37] Sander G., et al., 1975
[38] Shen V., et al., 1980
[39] Shpanchenko OV., et al., 1996
[40] Siegrist S., et al., 1985
[41] Siegrist S., et al., 1984
[42] Soung GY., et al., 2009
[43] Spierer P., et al., 1979
[44] Suryanarayana T. 1983
[45] Tewari DS., et al., 1983
[46] Traut RR., et al., 1995
[47] Traut RR., et al., 1983
[48] Yusupov MM., et al., 1986
External database links:  
DIP:
DIP-35914N
ECOCYC:
EG10868-MONOMER
ECOLIWIKI:
b3308
INTERPRO:
IPR031309
INTERPRO:
IPR031310
INTERPRO:
IPR022803
INTERPRO:
IPR020929
INTERPRO:
IPR002132
INTERPRO:
IPR020930
PANTHER:
PTHR11994
PDB:
1ML5
PDB:
2J28
PDB:
2RDO
PDB:
3BBX
PDB:
3J5L
PDB:
3J5S
PDB:
3J7Z
PDB:
3J8G
PDB:
3J9Y
PDB:
3J9Z
PDB:
3JA1
PDB:
3JBU
PDB:
3JBV
PDB:
3JCD
PDB:
3JCE
PDB:
3JCJ
PDB:
3JCN
PDB:
4CSU
PDB:
4U1U
PDB:
4U1V
PDB:
4U20
PDB:
4U24
PDB:
4U25
PDB:
4U26
PDB:
4U27
PDB:
4UY8
PDB:
4V47
PDB:
4V48
PDB:
4V4H
PDB:
4V4Q
PDB:
4V4V
PDB:
4V4W
PDB:
4V50
PDB:
4V52
PDB:
4V53
PDB:
4V54
PDB:
4V55
PDB:
4V56
PDB:
4V57
PDB:
4V5B
PDB:
4V5H
PDB:
4V5Y
PDB:
4V64
PDB:
4V65
PDB:
4V66
PDB:
4V69
PDB:
4V6C
PDB:
4V6D
PDB:
4V6E
PDB:
4V6K
PDB:
4V6L
PDB:
4V6M
PDB:
4V6N
PDB:
4V6O
PDB:
4V6P
PDB:
4V6Q
PDB:
4V6R
PDB:
4V6S
PDB:
4V6T
PDB:
4V6V
PDB:
4V6Y
PDB:
4V6Z
PDB:
4V70
PDB:
4V71
PDB:
4V72
PDB:
4V73
PDB:
4V74
PDB:
4V75
PDB:
4V76
PDB:
4V77
PDB:
4V78
PDB:
4V79
PDB:
4V7A
PDB:
4V7B
PDB:
4V7C
PDB:
4V7D
PDB:
4V7I
PDB:
4V7S
PDB:
4V7T
PDB:
4V7U
PDB:
4V7V
PDB:
4V85
PDB:
4V89
PDB:
4V9C
PDB:
4V9D
PDB:
4V9O
PDB:
4V9P
PDB:
4WF1
PDB:
4WOI
PDB:
4WWW
PDB:
4YBB
PDB:
5ADY
PDB:
5AFI
PDB:
5AKA
PDB:
5GAD
PDB:
5GAE
PDB:
5GAF
PDB:
5GAG
PDB:
5GAH
PDB:
5H5U
PDB:
5IQR
PDB:
5IT8
PDB:
5J5B
PDB:
5J7L
PDB:
5J88
PDB:
5J8A
PDB:
5J91
PDB:
5JC9
PDB:
5JTE
PDB:
5JU8
PDB:
5KCR
PDB:
5KCS
PDB:
5KPS
PDB:
5KPV
PDB:
5KPW
PDB:
5KPX
PDB:
5L3P
PDB:
5LZA
PDB:
5LZB
PDB:
5LZC
PDB:
5LZD
PDB:
5LZE
PDB:
5LZF
PDB:
5MDV
PDB:
5MDW
PDB:
5MDY
PDB:
5MDZ
PDB:
5MGP
PDB:
5NCO
PDB:
5NP6
PDB:
5NWY
PDB:
5O2R
PDB:
5U4I
PDB:
5U9F
PDB:
5U9G
PDB:
5UYK
PDB:
5UYL
PDB:
5UYM
PDB:
5UYN
PDB:
5UYP
PDB:
5UYQ
PDB:
5WDT
PDB:
5WE4
PDB:
5WE6
PDB:
5WFK
PDB:
6BU8
PDB:
6BY1
PDB:
6C4I
PDB:
6ENF
PDB:
6ENJ
PDB:
6ENU
PDB:
6GBZ
PDB:
6GC0
PDB:
6GC4
PDB:
6GC8
PDB:
6GWT
PDB:
6GXM
PDB:
6GXN
PDB:
6GXO
PDB:
6GXP
PDB:
6H4N
PDB:
6H58
PDB:
6HRM
PDB:
6I0Y
PDB:
6I7V
PDB:
6O9J
PDB:
6O9K
PDB:
6OFX
PDB:
6OG7
PDB:
6ORE
PDB:
6ORL
PDB:
6OST
PDB:
6OT3
PDB:
6OUO
PDB:
6Q97
PDB:
6Q98
PDB:
6Q9A
PDB:
6QUL
PDB:
6S0K
PDB:
6SZS
PDB:
6TBV
PDB:
6TC3
PFAM:
PF00673
PFAM:
PF00281
PRIDE:
P62399
PRODB:
PRO_000023813
PROSITE:
PS00358
REFSEQ:
NP_417767
SMR:
P62399
UNIPROT:
P62399


Operon      
Name: rplNXE-rpsNH-rplFR-rpsE-rpmD-rplO-secY-rpmJ         
Operon arrangement:
Transcription unit        Promoter
rplNXE-rpsNH-rplFR-rpsE-rpmD-rplO-secY-rpmJ


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_3752 3446641 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3753 3446790 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3754 (cluster) 3446794 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3755 (cluster) 3446797 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3756 3446801 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3757 3446807 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3758 3446812 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3759 (cluster) 3446829 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3760 (cluster) 3446832 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3761 (cluster) 3446837 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3762 (cluster) 3446840 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3763 3446845 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3764 3446851 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3765 3446872 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3766 3446880 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3767 (cluster) 3447230 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3768 (cluster) 3447242 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3769 3447245 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3770 3447267 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3771 (cluster) 3447453 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3772 3447455 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3773 3447457 reverse nd [RS-EPT-CBR] [49]
  promoter TSS_3774 (cluster) 3447461 reverse nd [RS-EPT-CBR] [49]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Abdurashidova GG., Tsvetkova EA., Budowsky EI., 1991, Direct tRNA-protein interactions in ribosomal complexes., Nucleic Acids Res 19(8):1909-15

 [2] Agrawal RK., Sharma MR., Kiel MC., Hirokawa G., Booth TM., Spahn CM., Grassucci RA., Kaji A., Frank J., 2004, Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications., Proc Natl Acad Sci U S A 101(24):8900-5

 [3] Andrieux E., Cozzone AJ., 1984, Conformational changes in bacterial polysomes induced by amino acid starvation., Int J Biochem 16(1):113-6

 [4] Bernabeu C., Vazquez D., Ballesta JP., 1976, Activities of protein-deficient particles derived from 50-S ribosomal subunits by NH4Cl/ethanol treatment., Eur J Biochem 69(1):233-41

 [5] Branlant C., Widada JS., Krol A., Ebel JP., 1977, Studies on the primary structure of the ribosomal 23S RNA of Escherichia coli: II. A characterisation and an alignment of 24 sections spanning the entire molecule and its application to the localisation of specific fragments., Nucleic Acids Res 4(12):4323-45

 [6] Cerretti DP., Dean D., Davis GR., Bedwell DM., Nomura M., 1983, The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene., Nucleic Acids Res 11(9):2599-616

 [7] Chang CN., Chang N., 1975, Methylation of the ribosomal proteins in Escherichia coli. Nature and stoichiometry of the methylated amino acids in 50S ribosomal proteins., Biochemistry 14(3):468-77

 [8] Chang FN., Chang CN., Paik WK., 1974, Methylation of ribosomal proteins in Escherichia coli., J Bacteriol 120(2):651-6

 [9] Chen R., Ehrke G., 1976, The primary structure of the 5 S RNA binding protein L5 of Escherichia coli ribosomes., FEBS Lett 69(1):240-5

 [10] Dabbs ER., 1977, A spectinomycin dependent mutant of Escherichia coli., Mol Gen Genet 151(3):261-7

 [11] Dey D., Bochkariov DE., Jokhadze GG., Traut RR., 1998, Cross-linking of selected residues in the N- and C-terminal domains of Escherichia coli protein L7/L12 to other ribosomal proteins and the effect of elongation factor Tu., J Biol Chem 273(3):1670-6

 [12] Dontsova OA., Efimov AV., Kopylov AM., 1990, [The 5S rRNA-protein complex of Escherichia coli studied by carbodiimide modification]., Nauchnye Doki Vyss Shkoly Biol Nauki (2):22-30

 [13] Fox JW., Wong KP., 1978, Changes in the conformation and stability of 5 S RNA upon the binding of ribosomal proteins., J Biol Chem 253(1):18-20

 [14] Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg SM., Van Roey P., Agrawal RK., Harvey SC., Sali A., Chapman MS., Frank J., 2003, Study of the structural dynamics of the E coli 70S ribosome using real-space refinement., Cell 113(6):789-801

 [15] Garrett RA., Noller HF., 1979, Structures of complexes of 5S RNA with ribosomal proteins L5, L18 and L25 from Escherichia coli: identification of kethoxal-reactive sites on the 5S RNA., J Mol Biol 132(4):637-48

 [16] Goringer HU., Wagner R., 1986, Construction and functional analysis of ribosomal 5S RNA from Escherichia coli with single base changes in the ribosomal protein binding sites., Biol Chem Hoppe Seyler 367(8):769-80

 [17] Herfurth E., Wittmann-Liebold B., 1995, Determination of peptide regions exposed at the surface of the bacterial ribosome with antibodies against synthetic peptides., Biol Chem Hoppe Seyler 376(2):81-90

 [18] Herold M., Nierhaus KH., 1987, Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes., J Biol Chem 262(18):8826-33

 [19] Isono K., Cumberlidge AG., Isono S., 1977, Further temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins., Mol Gen Genet 152(3):239-43

 [20] Jaskunas SR., Fallon AM., Nomura M., 1977, Identification and organization of ribosomal protein genes of Escherichia coli carried by lambdafus2 transducing phage., J Biol Chem 252(20):7323-36

 [21] Jaskunas SR., Nomura M., 1977, Organization of ribosomal protein genes of Escherichia coli as analyzed by polar insertion mutations., J Biol Chem 252(20):7337-43

 [22] Kakegawa T., Sato E., Hirose S., Igarashi K., 1986, Polyamine binding sites on Escherichia coli ribosomes., Arch Biochem Biophys 251(2):413-20

 [23] Kashiwagi K., Igarashi K., 1987, Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity., Biochim Biophys Acta 911(2):180-90

 [24] Kenny JW., Sommer A., Traut RR., 1975, Cross-linking studies on the 50 S ribosomal subunit of Escherichia coli with methyl 4-mercaptobutyrimidate., J Biol Chem 250(24):9434-6

 [25] Larrinua I., Delihas N., 1979, Accessibility of guanine at position 44 in the invariant sequence 5'CCG44AAC3' of Escherichia coli 5S RNA to reaction with kethoxal., Proc Natl Acad Sci U S A 76(9):4400-4

 [26] Lotti M., Noah M., Stoffler-Meilicke M., Stoffler G., 1989, Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy., Mol Gen Genet 216(2-3):245-53

 [27] Maimets TO., Ustav MB., Villems RL., Saarma MIu., Lind AIa., 1981, [Binding of Escherichia coli 50S ribosomal subunit proteins with two large 5S RNA fragments]., Mol Biol (Mosk) 15(3):569-74

 [28] Maly P., Wower J., Zobawa M., Brimacombe R., 1983, Identification of tyrosine residues that are susceptible to lactoperoxidase-catalyzed iodination on the surface of Escherichia coli 50s ribosomal subunits or 70s ribosomes., Biochemistry 22(13):3157-62

 [29] Meng J., Kanzaki G., Meas D., Lam CK., Crummer H., Tain J., Xu HH., 2012, A genome-wide inducible phenotypic screen identifies antisense RNA constructs silencing Escherichia coli essential genes., FEMS Microbiol Lett 329(1):45-53

 [30] Metspalu E., Ustav M., Maimets T., Villems R., 1982, The composition and properties of the Escherichia coli 5-S RNA-protein complex., Eur J Biochem 121(2):383-9

 [31] Morrison CA., Tischendorf G., Stoffler G., Garrett RA., 1977, Accessibility of proteins in 50S ribosomal subunits of Escherichia coli to antibodies: an ultracentrifugation study., Mol Gen Genet 151(3):245-52

 [32] Nag B., Tewari DS., Sommer A., Olson HM., Glitz DG., Traut RR., 1987, Probing ribosome function and the location of Escherichia coli ribosomal protein L5 with a monoclonal antibody., J Biol Chem 262(20):9681-7

 [33] Newberry V., Garrett RA., 1980, The role of the basic N-terminal region of protein L18 in 5S RNA-23S RNA complex formation., Nucleic Acids Res 8(18):4131-42

 [34] Osswald M., Greuer B., Brimacombe R., 1990, Localization of a series of RNA-protein cross-link sites in the 23S and 5S ribosomal RNA from Escherichia coli, induced by treatment of 50S subunits with three different bifunctional reagents., Nucleic Acids Res 18(23):6755-60

 [35] Randolph-Anderson BL., Gillham NW., Boynton JE., 1989, Electrophoretic and immunological comparisons of chloroplast and prokaryotic ribosomal proteins reveal that certain families of large subunit proteins are evolutionarily conserved., J Mol Evol 29(1):68-88

 [36] Redl B., Walleczek J., Stoffler-Meilicke M., Stoffler G., 1989, Immunoblotting analysis of protein-protein crosslinks within the 50S ribosomal subunit of Escherichia coli. A study using dimethylsuberimidate as crosslinking reagent., Eur J Biochem 181(2):351-6

 [37] Sander G., Marsh RC., Voigt J., Parmeggiani A., 1975, A comparative study of the 50S ribosomal subunit and several 50S subparticles in EF-T-and EF-G-dependent activities., Biochemistry 14(9):1805-14

 [38] Shen V., King TC., Kumar V., Daugherty B., 1980, Monoclonal antibodies to Escherichia coli 50S ribosomes., Nucleic Acids Res 8(20):4639-49

 [39] Shpanchenko OV., Zvereva MI., Dontsova OA., Nierhaus KH., Bogdanov AA., 1996, 5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins., FEBS Lett 394(1):71-5

 [40] Siegrist S., Moreau N., Le Goffic F., 1985, About the specificity of photoinduced affinity labeling of Escherichia coli ribosomes by dihydrorosaramicin, a macrolide related to erythromycin., Eur J Biochem 153(1):131-5

 [41] Siegrist S., Moreau N., Le Goffic F., 1984, [Photochemical affinity labeling of the macrolide binding site on the 70S E. coli ribosome]., C R Acad Sci III 299(3):49-51

 [42] Soung GY., Miller JL., Koc H., Koc EC., 2009, Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes., J Proteome Res 8(7):3390-402

 [43] Spierer P., Wang CC., Marsh TL., Zimmermann RA., 1979, Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichia coli., Nucleic Acids Res 6(4):1669-82

 [44] Suryanarayana T., 1983, Identification by affinity chromatography of Escherichia coli ribosomal proteins that bind erythromycin and chloramphenicol., Biochem Int 7(6):719-25

 [45] Tewari DS., Burma DP., 1983, Incorporation of 5S RNA into 16S-23S RNA complex., Biochem Biophys Res Commun 114(1):348-54

 [46] Traut RR., Dey D., Bochkariov DE., Oleinikov AV., Jokhadze GG., Hamman B., Jameson D., 1995, Location and domain structure of Escherichia coli ribosomal protein L7/L12: site specific cysteine crosslinking and attachment of fluorescent probes., Biochem Cell Biol 73(11-12):949-58

 [47] Traut RR., Lambert JM., Kenny JW., 1983, Ribosomal protein L7/L12 cross-links to proteins in separate regions of the 50 S ribosomal subunit of Escherichia coli., J Biol Chem 258(23):14592-8

 [48] Yusupov MM., Spirin AS., 1986, Are there proteins between the ribosomal subunits? Hot tritium bombardment experiments., FEBS Lett 197(1-2):229-33

 [49] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


RegulonDB