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P0ADY3

- RL14_ECOLI

UniProt

P0ADY3 - RL14_ECOLI

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Protein

50S ribosomal protein L14

Gene

rplN

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 (PubMed:12809609) 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. 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 (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.3 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

  1. large ribosomal subunit rRNA binding Source: EcoCyc
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
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.

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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10875. rplN.

Subcellular locationi

GO - Cellular componenti

  1. 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.

Expressioni

Gene expression databases

GenevestigatoriP0ADY3.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L19 (PubMed:2665813 and 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.

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 strandi4 – 1310
Beta strandi17 – 248
Beta strandi26 – 294
Beta strandi38 – 458
Beta strandi48 – 525
Beta strandi57 – 648
Beta strandi69 – 713
Helixi72 – 743
Beta strandi76 – 816
Beta strandi83 – 886
Turni89 – 913
Beta strandi92 – 954
Beta strandi97 – 993
Helixi105 – 1073
Turni110 – 1123
Helixi113 – 1175
Beta strandi118 – 1203

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00n1-122[»]
1P85electron microscopy12.30I1-123[»]
1P86electron microscopy11.50I1-123[»]
1VS6X-ray3.46K1-123[»]
1VS8X-ray3.46K1-123[»]
1VT2X-ray3.30K1-123[»]
2AW4X-ray3.46K1-123[»]
2AWBX-ray3.46K1-123[»]
2GYAelectron microscopy15.00I2-123[»]
2GYCelectron microscopy15.00I2-123[»]
2I2TX-ray3.22K1-123[»]
2I2VX-ray3.22K1-123[»]
2J28electron microscopy8.00K2-122[»]
2QAMX-ray3.21K1-123[»]
2QAOX-ray3.21K1-123[»]
2QBAX-ray3.54K1-123[»]
2QBCX-ray3.54K1-123[»]
2QBEX-ray3.30K1-123[»]
2QBGX-ray3.30K1-123[»]
2QBIX-ray4.00K1-123[»]
2QBKX-ray4.00K1-123[»]
2QOVX-ray3.93K1-123[»]
2QOXX-ray3.93K1-123[»]
2QOZX-ray3.50K1-123[»]
2QP1X-ray3.50K1-123[»]
2RDOelectron microscopy9.10K1-123[»]
2WWQelectron microscopy5.80K1-121[»]
2Z4LX-ray4.45K1-123[»]
2Z4NX-ray4.45K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3E1Belectron microscopy-D1-123[»]
3E1Delectron microscopy-D1-123[»]
3FIKelectron microscopy6.70K2-122[»]
3I1NX-ray3.19K1-123[»]
3I1PX-ray3.19K1-123[»]
3I1RX-ray3.81K1-123[»]
3I1TX-ray3.81K1-123[»]
3I20X-ray3.71K1-123[»]
3I22X-ray3.71K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZTelectron microscopy-L1-123[»]
3IZUelectron microscopy-L1-123[»]
3IZZelectron microscopy10.80G2-122[»]
3J01electron microscopy-K1-123[»]
3J0Telectron microscopy12.10M1-123[»]
3J0Welectron microscopy14.70M1-123[»]
3J0Yelectron microscopy13.50M1-123[»]
3J11electron microscopy13.10M1-123[»]
3J12electron microscopy11.50M1-123[»]
3J14electron microscopy11.50M1-123[»]
3J19electron microscopy8.30K1-122[»]
3J37electron microscopy9.80O1-123[»]
3J4Xelectron microscopy12.00K1-122[»]
3J50electron microscopy20.00K1-122[»]
3J51electron microscopy17.00K1-122[»]
3J52electron microscopy12.00K1-122[»]
3J54electron microscopy13.00K1-122[»]
3J56electron microscopy15.00K1-122[»]
3J58electron microscopy17.00K1-122[»]
3J5Aelectron microscopy12.00K1-122[»]
3J5Celectron microscopy17.00K1-122[»]
3J5Eelectron microscopy17.00K1-122[»]
3J5Gelectron microscopy20.00K1-122[»]
3J5Ielectron microscopy15.00K1-122[»]
3J5Kelectron microscopy9.00K1-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J5Oelectron microscopy6.80K1-123[»]
3J5Uelectron microscopy7.60M1-123[»]
3J5Welectron microscopy7.60N1-123[»]
3KCRelectron microscopy-K1-123[»]
3OASX-ray3.25K1-122[»]
3OATX-ray3.25K1-122[»]
3OFCX-ray3.19K1-122[»]
3OFDX-ray3.19K1-122[»]
3OFQX-ray3.10K1-122[»]
3OFRX-ray3.10K1-122[»]
3OFZX-ray3.29K1-122[»]
3OG0X-ray3.29K1-122[»]
3ORBX-ray3.30K1-123[»]
3R8SX-ray3.00K1-122[»]
3R8TX-ray3.00K1-122[»]
3SGFX-ray3.20O1-123[»]
3UOSX-ray3.70O1-123[»]
487Delectron microscopy7.50M1-122[»]
4CSUelectron microscopy5.50K1-123[»]
4GARX-ray3.30K1-123[»]
4GAUX-ray3.30K1-123[»]
4KIXX-ray2.90K1-123[»]
4KIZX-ray2.90K1-123[»]
4KJ1X-ray2.90K1-123[»]
4KJ3X-ray2.90K1-123[»]
4KJ5X-ray2.90K1-123[»]
4KJ7X-ray2.90K1-123[»]
4KJ9X-ray2.90K1-123[»]
4KJBX-ray2.90K1-123[»]
4PEBX-ray2.95K1-122[»]
4PECX-ray2.95K1-122[»]
4TOMX-ray3.00K1-122[»]
4TOOX-ray3.00K1-122[»]
4TOVX-ray2.90K1-122[»]
4TOXX-ray2.90K1-122[»]
4TP1X-ray2.90K1-122[»]
4TP3X-ray2.90K1-122[»]
4TP5X-ray2.90K1-122[»]
4TP7X-ray2.90K1-122[»]
4TP9X-ray2.80K1-122[»]
4TPBX-ray2.80K1-122[»]
4TPDX-ray2.80K1-122[»]
4TPFX-ray2.80K1-122[»]
ProteinModelPortaliP0ADY3.
SMRiP0ADY3. Positions 2-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADY3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0093.
HOGENOMiHOG000183702.
InParanoidiP0ADY3.
KOiK02874.
OMAiELRNDKF.
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:
EMBL
GenBank
DDBJ
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.
YP_492122.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76335; AAC76335; b3310.
BAE77981; BAE77981; BAE77981.
GeneIDi12934392.
947809.
KEGGiecj:Y75_p3866.
eco:b3310.
PATRICi32122052. VBIEscCol129921_3403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A65124. R5EC14.
RefSeqi NP_417769.1. NC_000913.3.
YP_492122.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML5 electron microscopy 14.00 n 1-122 [» ]
1P85 electron microscopy 12.30 I 1-123 [» ]
1P86 electron microscopy 11.50 I 1-123 [» ]
1VS6 X-ray 3.46 K 1-123 [» ]
1VS8 X-ray 3.46 K 1-123 [» ]
1VT2 X-ray 3.30 K 1-123 [» ]
2AW4 X-ray 3.46 K 1-123 [» ]
2AWB X-ray 3.46 K 1-123 [» ]
2GYA electron microscopy 15.00 I 2-123 [» ]
2GYC electron microscopy 15.00 I 2-123 [» ]
2I2T X-ray 3.22 K 1-123 [» ]
2I2V X-ray 3.22 K 1-123 [» ]
2J28 electron microscopy 8.00 K 2-122 [» ]
2QAM X-ray 3.21 K 1-123 [» ]
2QAO X-ray 3.21 K 1-123 [» ]
2QBA X-ray 3.54 K 1-123 [» ]
2QBC X-ray 3.54 K 1-123 [» ]
2QBE X-ray 3.30 K 1-123 [» ]
2QBG X-ray 3.30 K 1-123 [» ]
2QBI X-ray 4.00 K 1-123 [» ]
2QBK X-ray 4.00 K 1-123 [» ]
2QOV X-ray 3.93 K 1-123 [» ]
2QOX X-ray 3.93 K 1-123 [» ]
2QOZ X-ray 3.50 K 1-123 [» ]
2QP1 X-ray 3.50 K 1-123 [» ]
2RDO electron microscopy 9.10 K 1-123 [» ]
2WWQ electron microscopy 5.80 K 1-121 [» ]
2Z4L X-ray 4.45 K 1-123 [» ]
2Z4N X-ray 4.45 K 1-123 [» ]
3BBX electron microscopy 10.00 K 1-123 [» ]
3E1B electron microscopy - D 1-123 [» ]
3E1D electron microscopy - D 1-123 [» ]
3FIK electron microscopy 6.70 K 2-122 [» ]
3I1N X-ray 3.19 K 1-123 [» ]
3I1P X-ray 3.19 K 1-123 [» ]
3I1R X-ray 3.81 K 1-123 [» ]
3I1T X-ray 3.81 K 1-123 [» ]
3I20 X-ray 3.71 K 1-123 [» ]
3I22 X-ray 3.71 K 1-123 [» ]
3IY9 electron microscopy 14.10 K 2-122 [» ]
3IZT electron microscopy - L 1-123 [» ]
3IZU electron microscopy - L 1-123 [» ]
3IZZ electron microscopy 10.80 G 2-122 [» ]
3J01 electron microscopy - K 1-123 [» ]
3J0T electron microscopy 12.10 M 1-123 [» ]
3J0W electron microscopy 14.70 M 1-123 [» ]
3J0Y electron microscopy 13.50 M 1-123 [» ]
3J11 electron microscopy 13.10 M 1-123 [» ]
3J12 electron microscopy 11.50 M 1-123 [» ]
3J14 electron microscopy 11.50 M 1-123 [» ]
3J19 electron microscopy 8.30 K 1-122 [» ]
3J37 electron microscopy 9.80 O 1-123 [» ]
3J4X electron microscopy 12.00 K 1-122 [» ]
3J50 electron microscopy 20.00 K 1-122 [» ]
3J51 electron microscopy 17.00 K 1-122 [» ]
3J52 electron microscopy 12.00 K 1-122 [» ]
3J54 electron microscopy 13.00 K 1-122 [» ]
3J56 electron microscopy 15.00 K 1-122 [» ]
3J58 electron microscopy 17.00 K 1-122 [» ]
3J5A electron microscopy 12.00 K 1-122 [» ]
3J5C electron microscopy 17.00 K 1-122 [» ]
3J5E electron microscopy 17.00 K 1-122 [» ]
3J5G electron microscopy 20.00 K 1-122 [» ]
3J5I electron microscopy 15.00 K 1-122 [» ]
3J5K electron microscopy 9.00 K 1-122 [» ]
3J5L electron microscopy 6.60 K 1-122 [» ]
3J5O electron microscopy 6.80 K 1-123 [» ]
3J5U electron microscopy 7.60 M 1-123 [» ]
3J5W electron microscopy 7.60 N 1-123 [» ]
3KCR electron microscopy - K 1-123 [» ]
3OAS X-ray 3.25 K 1-122 [» ]
3OAT X-ray 3.25 K 1-122 [» ]
3OFC X-ray 3.19 K 1-122 [» ]
3OFD X-ray 3.19 K 1-122 [» ]
3OFQ X-ray 3.10 K 1-122 [» ]
3OFR X-ray 3.10 K 1-122 [» ]
3OFZ X-ray 3.29 K 1-122 [» ]
3OG0 X-ray 3.29 K 1-122 [» ]
3ORB X-ray 3.30 K 1-123 [» ]
3R8S X-ray 3.00 K 1-122 [» ]
3R8T X-ray 3.00 K 1-122 [» ]
3SGF X-ray 3.20 O 1-123 [» ]
3UOS X-ray 3.70 O 1-123 [» ]
487D electron microscopy 7.50 M 1-122 [» ]
4CSU electron microscopy 5.50 K 1-123 [» ]
4GAR X-ray 3.30 K 1-123 [» ]
4GAU X-ray 3.30 K 1-123 [» ]
4KIX X-ray 2.90 K 1-123 [» ]
4KIZ X-ray 2.90 K 1-123 [» ]
4KJ1 X-ray 2.90 K 1-123 [» ]
4KJ3 X-ray 2.90 K 1-123 [» ]
4KJ5 X-ray 2.90 K 1-123 [» ]
4KJ7 X-ray 2.90 K 1-123 [» ]
4KJ9 X-ray 2.90 K 1-123 [» ]
4KJB X-ray 2.90 K 1-123 [» ]
4PEB X-ray 2.95 K 1-122 [» ]
4PEC X-ray 2.95 K 1-122 [» ]
4TOM X-ray 3.00 K 1-122 [» ]
4TOO X-ray 3.00 K 1-122 [» ]
4TOV X-ray 2.90 K 1-122 [» ]
4TOX X-ray 2.90 K 1-122 [» ]
4TP1 X-ray 2.90 K 1-122 [» ]
4TP3 X-ray 2.90 K 1-122 [» ]
4TP5 X-ray 2.90 K 1-122 [» ]
4TP7 X-ray 2.90 K 1-122 [» ]
4TP9 X-ray 2.80 K 1-122 [» ]
4TPB X-ray 2.80 K 1-122 [» ]
4TPD X-ray 2.80 K 1-122 [» ]
4TPF X-ray 2.80 K 1-122 [» ]
ProteinModelPortali P0ADY3.
SMRi P0ADY3. Positions 2-123.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852121. 1 interaction.
DIPi DIP-35798N.
IntActi P0ADY3. 49 interactions.
MINTi MINT-1304553.
STRINGi 511145.b3310.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0ADY3.
PRIDEi P0ADY3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76335 ; AAC76335 ; b3310 .
BAE77981 ; BAE77981 ; BAE77981 .
GeneIDi 12934392.
947809.
KEGGi ecj:Y75_p3866.
eco:b3310.
PATRICi 32122052. VBIEscCol129921_3403.

Organism-specific databases

EchoBASEi EB0868.
EcoGenei EG10875. rplN.

Phylogenomic databases

eggNOGi COG0093.
HOGENOMi HOG000183702.
InParanoidi P0ADY3.
KOi K02874.
OMAi ELRNDKF.
OrthoDBi EOG6GBMJ6.
PhylomeDBi P0ADY3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10875-MONOMER.
ECOL316407:JW3272-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ADY3.
PROi P0ADY3.

Gene expression databases

Genevestigatori P0ADY3.

Family and domain databases

Gene3Di 2.40.150.20. 1 hit.
HAMAPi MF_01367. Ribosomal_L14.
InterProi IPR005745. Ribosomal_L14_bac-type.
IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view ]
PANTHERi PTHR11761. PTHR11761. 1 hit.
Pfami PF00238. Ribosomal_L14. 1 hit.
[Graphical view ]
SUPFAMi SSF50193. SSF50193. 1 hit.
TIGRFAMsi TIGR01067. rplN_bact. 1 hit.
PROSITEi PS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: October 29, 2014
This is version 91 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