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Protein

50S ribosomal protein L14

Gene

rplN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117).3 Publications
Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.1 Publication

GO - Molecular functioni

  • large ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10875-MONOMER.
ECOL316407:JW3272-MONOMER.

Protein family/group databases

MoonProtiP0ADY3.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L14UniRule annotation
Gene namesi
Name:rplNUniRule annotation
Ordered Locus Names:b3310, JW3272
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10875. rplN.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 971T → A: Reduced RsfS binding. 1 Publication
Mutagenesisi98 – 981R → A: Reduced RsfS binding. 1 Publication
Mutagenesisi114 – 1141K → A: Reduced RsfS binding. 1 Publication
Mutagenesisi117 – 1171S → A: No change in RsfS binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12312350S ribosomal protein L14PRO_0000128540Add
BLAST

Proteomic databases

PaxDbiP0ADY3.
PRIDEiP0ADY3.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L19 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association.2 Publications

Protein-protein interaction databases

BioGridi852121. 1 interaction.
DIPiDIP-35798N.
IntActiP0ADY3. 49 interactions.
MINTiMINT-1304553.
STRINGi511145.b3310.

Structurei

Secondary structure

1
123
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Beta strandi15 – 2410Combined sources
Beta strandi26 – 294Combined sources
Beta strandi38 – 469Combined sources
Beta strandi50 – 523Combined sources
Beta strandi57 – 648Combined sources
Beta strandi69 – 713Combined sources
Turni72 – 743Combined sources
Beta strandi76 – 816Combined sources
Beta strandi83 – 886Combined sources
Turni89 – 913Combined sources
Beta strandi92 – 954Combined sources
Beta strandi97 – 993Combined sources
Helixi105 – 1084Combined sources
Helixi110 – 1123Combined sources
Helixi113 – 1175Combined sources
Beta strandi118 – 1203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00n1-122[»]
2J28electron microscopy8.00K2-122[»]
2RDOelectron microscopy9.10K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZZelectron microscopy10.80G2-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J7Zelectron microscopy3.90K1-123[»]
3J9Yelectron microscopy3.90K1-123[»]
487Delectron microscopy7.50M1-122[»]
4CSUelectron microscopy5.50K1-123[»]
4U1UX-ray2.95BK/DK1-122[»]
4U1VX-ray3.00BK/DK1-122[»]
4U20X-ray2.90BK/DK1-122[»]
4U24X-ray2.90BK/DK1-122[»]
4U25X-ray2.90BK/DK1-122[»]
4U26X-ray2.80BK/DK1-122[»]
4U27X-ray2.80BK/DK1-122[»]
4UY8electron microscopy3.80K1-122[»]
4V47electron microscopy12.30AI1-123[»]
4V48electron microscopy11.50AI1-123[»]
4V4HX-ray3.46BK/DK1-123[»]
4V4QX-ray3.46BK/DK1-123[»]
4V4Velectron microscopy15.00BI2-123[»]
4V4Welectron microscopy15.00BI2-123[»]
4V50X-ray3.22BK/DK1-123[»]
4V52X-ray3.21BK/DK1-123[»]
4V53X-ray3.54BK/DK1-123[»]
4V54X-ray3.30BK/DK1-123[»]
4V55X-ray4.00BK/DK1-123[»]
4V56X-ray3.93BK/DK1-123[»]
4V57X-ray3.50BK/DK1-123[»]
4V5BX-ray3.74AK/CK1-123[»]
4V5Helectron microscopy5.80BK1-121[»]
4V5YX-ray4.45BK/DK1-123[»]
4V64X-ray3.50BK/DK1-123[»]
4V65electron microscopy9.00BD1-123[»]
4V66electron microscopy9.00BD1-123[»]
4V69electron microscopy6.70BK2-122[»]
4V6CX-ray3.19BK/DK1-123[»]
4V6DX-ray3.81BK/DK1-123[»]
4V6EX-ray3.71BK/DK1-123[»]
4V6Kelectron microscopy8.25AL1-123[»]
4V6Lelectron microscopy13.20BL1-123[»]
4V6Melectron microscopy7.10BK1-123[»]
4V6Nelectron microscopy12.10AM1-123[»]
4V6Oelectron microscopy14.70BM1-123[»]
4V6Pelectron microscopy13.50BM1-123[»]
4V6Qelectron microscopy11.50BM1-123[»]
4V6Relectron microscopy11.50BM1-123[»]
4V6Selectron microscopy13.10AM1-123[»]
4V6Telectron microscopy8.30BK1-122[»]
4V6Velectron microscopy9.80BO1-123[»]
4V6Yelectron microscopy12.00BK1-122[»]
4V6Zelectron microscopy12.00BK1-122[»]
4V70electron microscopy17.00BK1-122[»]
4V71electron microscopy20.00BK1-122[»]
4V72electron microscopy13.00BK1-122[»]
4V73electron microscopy15.00BK1-122[»]
4V74electron microscopy17.00BK1-122[»]
4V75electron microscopy12.00BK1-122[»]
4V76electron microscopy17.00BK1-122[»]
4V77electron microscopy17.00BK1-122[»]
4V78electron microscopy20.00BK1-122[»]
4V79electron microscopy15.00BK1-122[»]
4V7Aelectron microscopy9.00BK1-122[»]
4V7Belectron microscopy6.80BK1-123[»]
4V7Celectron microscopy7.60BM1-123[»]
4V7Delectron microscopy7.60AN1-123[»]
4V7Ielectron microscopy9.60AK1-123[»]
4V7SX-ray3.25BK/DK1-122[»]
4V7TX-ray3.19BK/DK1-122[»]
4V7UX-ray3.10BK/DK1-122[»]
4V7VX-ray3.29BK/DK1-122[»]
4V85X-ray3.20O1-123[»]
4V89X-ray3.70BO1-123[»]
4V9CX-ray3.30BK/DK1-123[»]
4V9DX-ray3.00CK/DK1-122[»]
4V9OX-ray2.90AK/CK/EK/GK1-123[»]
4V9PX-ray2.90AK/CK/EK/GK1-123[»]
4WF1X-ray3.09BK/DK1-122[»]
4WWWX-ray3.10RK/YK1-122[»]
4YBBX-ray2.10CL/DL1-123[»]
5AFIelectron microscopy2.90K1-123[»]
5AKAelectron microscopy5.70K1-123[»]
ProteinModelPortaliP0ADY3.
SMRiP0ADY3. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADY3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0093.
HOGENOMiHOG000183702.
InParanoidiP0ADY3.
KOiK02874.
OMAiRKVQCIK.
OrthoDBiEOG6GBMJ6.
PhylomeDBiP0ADY3.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR005745. Ribosomal_L14_bac-type.
IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
TIGRFAMsiTIGR01067. rplN_bact. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ADY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG
60 70 80 90 100
KVKKGDVLKA VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF
110 120
GPVTRELRSE KFMKIISLAP EVL
Length:123
Mass (Da):13,541
Last modified:April 1, 1988 - v1
Checksum:i192ACB1623979510
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631Missing AA sequence (PubMed:352727).Curated
Sequence conflicti84 – 841C → S AA sequence (PubMed:352727).Curated
Sequence conflicti90 – 912NS → TD AA sequence (PubMed:352727).Curated
Sequence conflicti97 – 971Missing AA sequence (PubMed:352727).Curated
Sequence conflicti115 – 1151I → L AA sequence (PubMed:352727).Curated
Sequence conflicti123 – 1231Missing AA sequence (PubMed:352727).Curated

Mass spectrometryi

Molecular mass is 13540.2 Da from positions 1 - 123. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25715.1.
U18997 Genomic DNA. Translation: AAA58107.1.
U00096 Genomic DNA. Translation: AAC76335.1.
AP009048 Genomic DNA. Translation: BAE77981.1.
V00357 Genomic DNA. Translation: CAA23653.1.
PIRiA65124. R5EC14.
RefSeqiNP_417769.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76335; AAC76335; b3310.
BAE77981; BAE77981; BAE77981.
GeneIDi947809.
KEGGiecj:Y75_p3866.
eco:b3310.
PATRICi32122052. VBIEscCol129921_3403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25715.1.
U18997 Genomic DNA. Translation: AAA58107.1.
U00096 Genomic DNA. Translation: AAC76335.1.
AP009048 Genomic DNA. Translation: BAE77981.1.
V00357 Genomic DNA. Translation: CAA23653.1.
PIRiA65124. R5EC14.
RefSeqiNP_417769.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00n1-122[»]
2J28electron microscopy8.00K2-122[»]
2RDOelectron microscopy9.10K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZZelectron microscopy10.80G2-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J7Zelectron microscopy3.90K1-123[»]
3J9Yelectron microscopy3.90K1-123[»]
487Delectron microscopy7.50M1-122[»]
4CSUelectron microscopy5.50K1-123[»]
4U1UX-ray2.95BK/DK1-122[»]
4U1VX-ray3.00BK/DK1-122[»]
4U20X-ray2.90BK/DK1-122[»]
4U24X-ray2.90BK/DK1-122[»]
4U25X-ray2.90BK/DK1-122[»]
4U26X-ray2.80BK/DK1-122[»]
4U27X-ray2.80BK/DK1-122[»]
4UY8electron microscopy3.80K1-122[»]
4V47electron microscopy12.30AI1-123[»]
4V48electron microscopy11.50AI1-123[»]
4V4HX-ray3.46BK/DK1-123[»]
4V4QX-ray3.46BK/DK1-123[»]
4V4Velectron microscopy15.00BI2-123[»]
4V4Welectron microscopy15.00BI2-123[»]
4V50X-ray3.22BK/DK1-123[»]
4V52X-ray3.21BK/DK1-123[»]
4V53X-ray3.54BK/DK1-123[»]
4V54X-ray3.30BK/DK1-123[»]
4V55X-ray4.00BK/DK1-123[»]
4V56X-ray3.93BK/DK1-123[»]
4V57X-ray3.50BK/DK1-123[»]
4V5BX-ray3.74AK/CK1-123[»]
4V5Helectron microscopy5.80BK1-121[»]
4V5YX-ray4.45BK/DK1-123[»]
4V64X-ray3.50BK/DK1-123[»]
4V65electron microscopy9.00BD1-123[»]
4V66electron microscopy9.00BD1-123[»]
4V69electron microscopy6.70BK2-122[»]
4V6CX-ray3.19BK/DK1-123[»]
4V6DX-ray3.81BK/DK1-123[»]
4V6EX-ray3.71BK/DK1-123[»]
4V6Kelectron microscopy8.25AL1-123[»]
4V6Lelectron microscopy13.20BL1-123[»]
4V6Melectron microscopy7.10BK1-123[»]
4V6Nelectron microscopy12.10AM1-123[»]
4V6Oelectron microscopy14.70BM1-123[»]
4V6Pelectron microscopy13.50BM1-123[»]
4V6Qelectron microscopy11.50BM1-123[»]
4V6Relectron microscopy11.50BM1-123[»]
4V6Selectron microscopy13.10AM1-123[»]
4V6Telectron microscopy8.30BK1-122[»]
4V6Velectron microscopy9.80BO1-123[»]
4V6Yelectron microscopy12.00BK1-122[»]
4V6Zelectron microscopy12.00BK1-122[»]
4V70electron microscopy17.00BK1-122[»]
4V71electron microscopy20.00BK1-122[»]
4V72electron microscopy13.00BK1-122[»]
4V73electron microscopy15.00BK1-122[»]
4V74electron microscopy17.00BK1-122[»]
4V75electron microscopy12.00BK1-122[»]
4V76electron microscopy17.00BK1-122[»]
4V77electron microscopy17.00BK1-122[»]
4V78electron microscopy20.00BK1-122[»]
4V79electron microscopy15.00BK1-122[»]
4V7Aelectron microscopy9.00BK1-122[»]
4V7Belectron microscopy6.80BK1-123[»]
4V7Celectron microscopy7.60BM1-123[»]
4V7Delectron microscopy7.60AN1-123[»]
4V7Ielectron microscopy9.60AK1-123[»]
4V7SX-ray3.25BK/DK1-122[»]
4V7TX-ray3.19BK/DK1-122[»]
4V7UX-ray3.10BK/DK1-122[»]
4V7VX-ray3.29BK/DK1-122[»]
4V85X-ray3.20O1-123[»]
4V89X-ray3.70BO1-123[»]
4V9CX-ray3.30BK/DK1-123[»]
4V9DX-ray3.00CK/DK1-122[»]
4V9OX-ray2.90AK/CK/EK/GK1-123[»]
4V9PX-ray2.90AK/CK/EK/GK1-123[»]
4WF1X-ray3.09BK/DK1-122[»]
4WWWX-ray3.10RK/YK1-122[»]
4YBBX-ray2.10CL/DL1-123[»]
5AFIelectron microscopy2.90K1-123[»]
5AKAelectron microscopy5.70K1-123[»]
ProteinModelPortaliP0ADY3.
SMRiP0ADY3. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852121. 1 interaction.
DIPiDIP-35798N.
IntActiP0ADY3. 49 interactions.
MINTiMINT-1304553.
STRINGi511145.b3310.

Chemistry

ChEMBLiCHEMBL2363135.

Protein family/group databases

MoonProtiP0ADY3.

Proteomic databases

PaxDbiP0ADY3.
PRIDEiP0ADY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76335; AAC76335; b3310.
BAE77981; BAE77981; BAE77981.
GeneIDi947809.
KEGGiecj:Y75_p3866.
eco:b3310.
PATRICi32122052. VBIEscCol129921_3403.

Organism-specific databases

EchoBASEiEB0868.
EcoGeneiEG10875. rplN.

Phylogenomic databases

eggNOGiCOG0093.
HOGENOMiHOG000183702.
InParanoidiP0ADY3.
KOiK02874.
OMAiRKVQCIK.
OrthoDBiEOG6GBMJ6.
PhylomeDBiP0ADY3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10875-MONOMER.
ECOL316407:JW3272-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ADY3.
PROiP0ADY3.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR005745. Ribosomal_L14_bac-type.
IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
TIGRFAMsiTIGR01067. rplN_bact. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of protein L14 isolated from Escherichia coli ribosomes."
    Morinaga T., Funatsu G., Funatsu M., Wittmann-Liebold B., Wittmann H.G.
    FEBS Lett. 91:74-77(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K.
  2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli."
    Post L.E., Arfsten A.E., Reusser F., Nomura M.
    Cell 15:215-229(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    Strain: K12.
  6. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
    Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
    EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-28, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  7. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
    Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
    Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO L19.
  8. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  9. Cited for: FUNCTION, INTERACTION WITH RSFS, MUTAGENESIS OF THR-97; ARG-98; LYS-114 AND SER-117.
    Strain: K12 / MG1655 / ATCC 47076.
  10. "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
    Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
    J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  11. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), INTERSUBUNIT BRIDGE FORMATION.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  13. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 1-122 IN TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL14_ECOLI
AccessioniPrimary (citable) accession number: P0ADY3
Secondary accession number(s): P02411, Q2M6X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 24, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.