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P0A7J7

- RL11_ECOLI

UniProt

P0A7J7 - RL11_ECOLI

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Protein
50S ribosomal protein L11
Gene
rplK, relC, b3983, JW3946
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.UniRule annotation

GO - Molecular functioni

  1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP
  2. protein binding Source: IntAct
  3. rRNA binding Source: EcoCyc
  4. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. stringent response Source: EcoCyc
  2. translational termination Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10872-MONOMER.
ECOL316407:JW3946-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L11
Gene namesi
Name:rplK
Synonyms:relC
Ordered Locus Names:b3983, JW3946
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10872. rplK.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 14214150S ribosomal protein L11UniRule annotation
PRO_0000104283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N,N-trimethylalanineUniRule annotation
Modified residuei4 – 41N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei40 – 401N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei72 – 721N6-succinyllysine1 Publication
Modified residuei81 – 811N6-succinyllysine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP0A7J7.
PRIDEiP0A7J7.

Expressioni

Gene expression databases

GenevestigatoriP0A7J7.

Interactioni

Subunit structurei

Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.

Binary interactionsi

WithEntry#Exp.IntActNotes
prmAP0A8T13EBI-547288,EBI-556300

Protein-protein interaction databases

BioGridi852778. 1 interaction.
DIPiDIP-35882N.
IntActiP0A7J7. 46 interactions.
MINTiMINT-1232893.
STRINGi511145.b3983.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83
Beta strandi9 – 135
Beta strandi15 – 195
Beta strandi21 – 244
Helixi25 – 284
Beta strandi29 – 324
Helixi35 – 373
Turni38 – 403
Helixi42 – 443
Turni45 – 495
Beta strandi51 – 533
Beta strandi55 – 617
Beta strandi62 – 665
Beta strandi67 – 715
Turni76 – 849
Beta strandi87 – 893
Beta strandi94 – 963
Beta strandi100 – 1045
Turni105 – 1073
Helixi108 – 1114
Helixi112 – 1165
Beta strandi120 – 1223
Helixi124 – 1329
Beta strandi134 – 1363
Beta strandi139 – 1413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50K1-140[»]
1MJ1electron microscopy13.00L1-141[»]
1ML5electron microscopy14.00l1-141[»]
1P85electron microscopy12.30G2-142[»]
1P86electron microscopy11.50G2-142[»]
1VS6X-ray3.46I1-142[»]
1VS8X-ray3.46I1-142[»]
1VT2X-ray3.30I1-142[»]
2AW4X-ray3.46I2-142[»]
2AWBX-ray3.46I2-142[»]
2GYAelectron microscopy15.00G3-141[»]
2GYCelectron microscopy15.00G3-141[»]
2I2TX-ray3.22I2-142[»]
2I2VX-ray3.22I2-142[»]
2J28electron microscopy8.00I2-142[»]
2QAMX-ray3.21I2-142[»]
2QAOX-ray3.21I2-142[»]
2QBAX-ray3.54I2-142[»]
2QBCX-ray3.54I2-142[»]
2QBEX-ray3.30I2-142[»]
2QBGX-ray3.30I2-142[»]
2QBIX-ray4.00I2-142[»]
2QBKX-ray4.00I2-142[»]
2QOVX-ray3.93I2-142[»]
2QOXX-ray3.93I2-142[»]
2QOZX-ray3.50I2-142[»]
2QP1X-ray3.50I2-142[»]
2RDOelectron microscopy9.10I2-142[»]
2VHMX-ray3.74I2-142[»]
2VHNX-ray3.74I2-142[»]
2WWQelectron microscopy5.80I2-142[»]
2Z4LX-ray4.45I2-142[»]
2Z4NX-ray4.45I2-142[»]
3DEGelectron microscopy-H2-142[»]
3DF2X-ray3.50I2-141[»]
3DF4X-ray3.50I2-141[»]
3E1Belectron microscopy-51-142[»]
3E1Delectron microscopy-51-142[»]
3EP2electron microscopy-I2-142[»]
3EQ3electron microscopy-I2-142[»]
3EQ4electron microscopy-I2-142[»]
3FIKelectron microscopy6.70I2-142[»]
3I1NX-ray3.19I1-142[»]
3I1PX-ray3.19I1-142[»]
3I1RX-ray3.81I1-142[»]
3I1TX-ray3.81I1-142[»]
3I20X-ray3.71I1-142[»]
3I22X-ray3.71I1-142[»]
3IZTelectron microscopy-J1-142[»]
3IZUelectron microscopy-J1-142[»]
3J01electron microscopy-I2-142[»]
3J0Delectron microscopy11.10G2-142[»]
3J0Telectron microscopy12.10K2-142[»]
3J0Welectron microscopy14.70K2-142[»]
3J0Yelectron microscopy13.50K2-142[»]
3J11electron microscopy13.10K2-142[»]
3J12electron microscopy11.50K2-142[»]
3J14electron microscopy11.50K2-142[»]
3J19electron microscopy8.30I2-142[»]
3J37electron microscopy9.80K2-142[»]
3J4Xelectron microscopy12.00I1-142[»]
3J50electron microscopy20.00I1-142[»]
3J51electron microscopy17.00I1-142[»]
3J52electron microscopy12.00I1-142[»]
3J54electron microscopy13.00I1-142[»]
3J56electron microscopy15.00I1-142[»]
3J58electron microscopy17.00I1-142[»]
3J5Aelectron microscopy12.00I1-142[»]
3J5Celectron microscopy17.00I1-142[»]
3J5Eelectron microscopy17.00I1-142[»]
3J5Gelectron microscopy20.00I1-142[»]
3J5Ielectron microscopy15.00I1-142[»]
3J5Kelectron microscopy9.00I1-142[»]
3J5Lelectron microscopy6.60I2-142[»]
3J5Oelectron microscopy6.80I1-142[»]
3J5Uelectron microscopy7.60K2-142[»]
3J5Welectron microscopy7.60K2-142[»]
3KCRelectron microscopy-I1-142[»]
3OASX-ray3.25I2-142[»]
3OATX-ray3.25I2-142[»]
3OFCX-ray3.19I2-142[»]
3OFDX-ray3.19I2-142[»]
3OFQX-ray3.10I2-142[»]
3OFRX-ray3.10I2-142[»]
3OFZX-ray3.29I2-142[»]
3OG0X-ray3.29I2-142[»]
3ORBX-ray3.30I1-142[»]
3R8SX-ray3.00I2-142[»]
3R8TX-ray3.00I2-142[»]
3SGFX-ray3.20I1-142[»]
3UOSX-ray3.70I1-142[»]
487Delectron microscopy7.50L10-86[»]
4CSUelectron microscopy5.50I2-142[»]
4GARX-ray3.30I1-142[»]
4GAUX-ray3.30I1-142[»]
4KIXX-ray2.90I1-142[»]
4KIZX-ray2.90I1-142[»]
4KJ1X-ray2.90I1-142[»]
4KJ3X-ray2.90I1-142[»]
4KJ5X-ray2.90I1-142[»]
4KJ7X-ray2.90I1-142[»]
4KJ9X-ray2.90I1-142[»]
4KJBX-ray2.90I1-142[»]
ProteinModelPortaliP0A7J7.
SMRiP0A7J7. Positions 3-141.

Miscellaneous databases

EvolutionaryTraceiP0A7J7.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0080.
HOGENOMiHOG000082123.
KOiK02867.
OMAiIEAYIKL.
OrthoDBiEOG69PQ9D.
PhylomeDBiP0A7J7.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsiTIGR01632. L11_bact. 1 hit.
PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7J7-1 [UniParc]FASTAAdd to Basket

« Hide

MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE    50
KGLPIPVVIT VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK 100
ISRAQLQEIA QTKAADMTGA DIEAMTRSIE GTARSMGLVV ED 142
Length:142
Mass (Da):14,875
Last modified:January 23, 2007 - v2
Checksum:iC49226BB2462BE0F
GO

Mass spectrometryi

Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.
PIRiS12572. R5EC11.
RefSeqiNP_418410.1. NC_000913.3.
YP_491478.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76957; AAC76957; b3983.
BAE77337; BAE77337; BAE77337.
GeneIDi12930523.
948484.
KEGGiecj:Y75_p3214.
eco:b3983.
PATRICi32123487. VBIEscCol129921_4096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00339 Genomic DNA. Translation: CAA23621.1 . Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1 .
U00006 Genomic DNA. Translation: AAC43081.1 .
U00096 Genomic DNA. Translation: AAC76957.1 .
AP009048 Genomic DNA. Translation: BAE77337.1 .
PIRi S12572. R5EC11.
RefSeqi NP_418410.1. NC_000913.3.
YP_491478.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG0 electron microscopy 11.50 K 1-140 [» ]
1MJ1 electron microscopy 13.00 L 1-141 [» ]
1ML5 electron microscopy 14.00 l 1-141 [» ]
1P85 electron microscopy 12.30 G 2-142 [» ]
1P86 electron microscopy 11.50 G 2-142 [» ]
1VS6 X-ray 3.46 I 1-142 [» ]
1VS8 X-ray 3.46 I 1-142 [» ]
1VT2 X-ray 3.30 I 1-142 [» ]
2AW4 X-ray 3.46 I 2-142 [» ]
2AWB X-ray 3.46 I 2-142 [» ]
2GYA electron microscopy 15.00 G 3-141 [» ]
2GYC electron microscopy 15.00 G 3-141 [» ]
2I2T X-ray 3.22 I 2-142 [» ]
2I2V X-ray 3.22 I 2-142 [» ]
2J28 electron microscopy 8.00 I 2-142 [» ]
2QAM X-ray 3.21 I 2-142 [» ]
2QAO X-ray 3.21 I 2-142 [» ]
2QBA X-ray 3.54 I 2-142 [» ]
2QBC X-ray 3.54 I 2-142 [» ]
2QBE X-ray 3.30 I 2-142 [» ]
2QBG X-ray 3.30 I 2-142 [» ]
2QBI X-ray 4.00 I 2-142 [» ]
2QBK X-ray 4.00 I 2-142 [» ]
2QOV X-ray 3.93 I 2-142 [» ]
2QOX X-ray 3.93 I 2-142 [» ]
2QOZ X-ray 3.50 I 2-142 [» ]
2QP1 X-ray 3.50 I 2-142 [» ]
2RDO electron microscopy 9.10 I 2-142 [» ]
2VHM X-ray 3.74 I 2-142 [» ]
2VHN X-ray 3.74 I 2-142 [» ]
2WWQ electron microscopy 5.80 I 2-142 [» ]
2Z4L X-ray 4.45 I 2-142 [» ]
2Z4N X-ray 4.45 I 2-142 [» ]
3DEG electron microscopy - H 2-142 [» ]
3DF2 X-ray 3.50 I 2-141 [» ]
3DF4 X-ray 3.50 I 2-141 [» ]
3E1B electron microscopy - 5 1-142 [» ]
3E1D electron microscopy - 5 1-142 [» ]
3EP2 electron microscopy - I 2-142 [» ]
3EQ3 electron microscopy - I 2-142 [» ]
3EQ4 electron microscopy - I 2-142 [» ]
3FIK electron microscopy 6.70 I 2-142 [» ]
3I1N X-ray 3.19 I 1-142 [» ]
3I1P X-ray 3.19 I 1-142 [» ]
3I1R X-ray 3.81 I 1-142 [» ]
3I1T X-ray 3.81 I 1-142 [» ]
3I20 X-ray 3.71 I 1-142 [» ]
3I22 X-ray 3.71 I 1-142 [» ]
3IZT electron microscopy - J 1-142 [» ]
3IZU electron microscopy - J 1-142 [» ]
3J01 electron microscopy - I 2-142 [» ]
3J0D electron microscopy 11.10 G 2-142 [» ]
3J0T electron microscopy 12.10 K 2-142 [» ]
3J0W electron microscopy 14.70 K 2-142 [» ]
3J0Y electron microscopy 13.50 K 2-142 [» ]
3J11 electron microscopy 13.10 K 2-142 [» ]
3J12 electron microscopy 11.50 K 2-142 [» ]
3J14 electron microscopy 11.50 K 2-142 [» ]
3J19 electron microscopy 8.30 I 2-142 [» ]
3J37 electron microscopy 9.80 K 2-142 [» ]
3J4X electron microscopy 12.00 I 1-142 [» ]
3J50 electron microscopy 20.00 I 1-142 [» ]
3J51 electron microscopy 17.00 I 1-142 [» ]
3J52 electron microscopy 12.00 I 1-142 [» ]
3J54 electron microscopy 13.00 I 1-142 [» ]
3J56 electron microscopy 15.00 I 1-142 [» ]
3J58 electron microscopy 17.00 I 1-142 [» ]
3J5A electron microscopy 12.00 I 1-142 [» ]
3J5C electron microscopy 17.00 I 1-142 [» ]
3J5E electron microscopy 17.00 I 1-142 [» ]
3J5G electron microscopy 20.00 I 1-142 [» ]
3J5I electron microscopy 15.00 I 1-142 [» ]
3J5K electron microscopy 9.00 I 1-142 [» ]
3J5L electron microscopy 6.60 I 2-142 [» ]
3J5O electron microscopy 6.80 I 1-142 [» ]
3J5U electron microscopy 7.60 K 2-142 [» ]
3J5W electron microscopy 7.60 K 2-142 [» ]
3KCR electron microscopy - I 1-142 [» ]
3OAS X-ray 3.25 I 2-142 [» ]
3OAT X-ray 3.25 I 2-142 [» ]
3OFC X-ray 3.19 I 2-142 [» ]
3OFD X-ray 3.19 I 2-142 [» ]
3OFQ X-ray 3.10 I 2-142 [» ]
3OFR X-ray 3.10 I 2-142 [» ]
3OFZ X-ray 3.29 I 2-142 [» ]
3OG0 X-ray 3.29 I 2-142 [» ]
3ORB X-ray 3.30 I 1-142 [» ]
3R8S X-ray 3.00 I 2-142 [» ]
3R8T X-ray 3.00 I 2-142 [» ]
3SGF X-ray 3.20 I 1-142 [» ]
3UOS X-ray 3.70 I 1-142 [» ]
487D electron microscopy 7.50 L 10-86 [» ]
4CSU electron microscopy 5.50 I 2-142 [» ]
4GAR X-ray 3.30 I 1-142 [» ]
4GAU X-ray 3.30 I 1-142 [» ]
4KIX X-ray 2.90 I 1-142 [» ]
4KIZ X-ray 2.90 I 1-142 [» ]
4KJ1 X-ray 2.90 I 1-142 [» ]
4KJ3 X-ray 2.90 I 1-142 [» ]
4KJ5 X-ray 2.90 I 1-142 [» ]
4KJ7 X-ray 2.90 I 1-142 [» ]
4KJ9 X-ray 2.90 I 1-142 [» ]
4KJB X-ray 2.90 I 1-142 [» ]
ProteinModelPortali P0A7J7.
SMRi P0A7J7. Positions 3-141.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852778. 1 interaction.
DIPi DIP-35882N.
IntActi P0A7J7. 46 interactions.
MINTi MINT-1232893.
STRINGi 511145.b3983.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7J7.
PRIDEi P0A7J7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76957 ; AAC76957 ; b3983 .
BAE77337 ; BAE77337 ; BAE77337 .
GeneIDi 12930523.
948484.
KEGGi ecj:Y75_p3214.
eco:b3983.
PATRICi 32123487. VBIEscCol129921_4096.

Organism-specific databases

EchoBASEi EB0865.
EcoGenei EG10872. rplK.

Phylogenomic databases

eggNOGi COG0080.
HOGENOMi HOG000082123.
KOi K02867.
OMAi IEAYIKL.
OrthoDBi EOG69PQ9D.
PhylomeDBi P0A7J7.

Enzyme and pathway databases

BioCyci EcoCyc:EG10872-MONOMER.
ECOL316407:JW3946-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7J7.
PROi P0A7J7.

Gene expression databases

Genevestigatori P0A7J7.

Family and domain databases

Gene3Di 1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPi MF_00736. Ribosomal_L11.
InterProi IPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view ]
PANTHERi PTHR11661. PTHR11661. 1 hit.
Pfami PF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view ]
SMARTi SM00649. RL11. 1 hit.
[Graphical view ]
SUPFAMi SSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsi TIGR01632. L11_bact. 1 hit.
PROSITEi PS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
    Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
    Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes."
    Dognin M.J., Wittmann-Liebold B.
    Eur. J. Biochem. 112:131-151(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-142.
    Strain: K12.
  6. "Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
    Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
    J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
  7. "Structural properties of ribosomal protein L11 from Escherichia coli."
    Choli T.
    Biochem. Int. 19:1323-1338(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURAL STUDIES.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "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.
  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. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-72 AND LYS-81.
    Strain: K12.
  12. "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).
    Strain: MRE-600.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL11_ECOLI
AccessioniPrimary (citable) accession number: P0A7J7
Secondary accession number(s): P02409, P76778, Q2M8R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 98 of the entry and version 2 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

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