Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P60624

- RL24_ECOLI

UniProt

P60624 - RL24_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

50S ribosomal protein L24

Gene

rplX

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

Functioni

One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.1 Publication
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.1 Publication

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10884-MONOMER.
ECOL316407:JW3271-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L24
Gene namesi
Name:rplX
Ordered Locus Names:b3309, JW3271
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10884. rplX.

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 – 10410350S ribosomal protein L24PRO_0000130654Add
BLAST

Proteomic databases

PaxDbiP60624.
PRIDEiP60624.

Expressioni

Gene expression databases

GenevestigatoriP60624.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Might contact the SecYEG translocation complex when it is docked with the ribosome.

Binary interactionsi

WithEntry#Exp.IntActNotes
phoBP0AFJ51EBI-546481,EBI-1116564

Protein-protein interaction databases

DIPiDIP-47846N.
IntActiP60624. 51 interactions.
MINTiMINT-1294921.
STRINGi511145.b3309.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi15 – 184Combined sources
Beta strandi22 – 287Combined sources
Beta strandi32 – 365Combined sources
Beta strandi39 – 468Combined sources
Beta strandi50 – 534Combined sources
Beta strandi57 – 626Combined sources
Helixi67 – 693Combined sources
Beta strandi70 – 734Combined sources
Beta strandi75 – 773Combined sources
Beta strandi78 – 814Combined sources
Beta strandi83 – 853Combined sources
Beta strandi88 – 914Combined sources
Beta strandi94 – 963Combined sources
Turni97 – 1004Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00u2-104[»]
1P85electron microscopy12.30S2-104[»]
1P86electron microscopy11.50S2-104[»]
1VS6X-ray3.46U1-104[»]
1VS8X-ray3.46U1-104[»]
1VT2X-ray3.30U1-104[»]
2AW4X-ray3.46U2-104[»]
2AWBX-ray3.46U2-104[»]
2GYAelectron microscopy15.00S4-102[»]
2GYCelectron microscopy15.00S4-102[»]
2I2TX-ray3.22U2-104[»]
2I2VX-ray3.22U2-104[»]
2J28electron microscopy8.00U2-103[»]
2QAMX-ray3.21U2-104[»]
2QAOX-ray3.21U2-104[»]
2QBAX-ray3.54U2-104[»]
2QBCX-ray3.54U2-104[»]
2QBEX-ray3.30U2-104[»]
2QBGX-ray3.30U2-104[»]
2QBIX-ray4.00U2-104[»]
2QBKX-ray4.00U2-104[»]
2QOVX-ray3.93U2-104[»]
2QOXX-ray3.93U2-104[»]
2QOZX-ray3.50U2-104[»]
2QP1X-ray3.50U2-104[»]
2RDOelectron microscopy9.10U2-104[»]
2VHMX-ray3.74U2-104[»]
2VHNX-ray3.74U2-104[»]
2VRHelectron microscopy19.00C2-104[»]
2WWQelectron microscopy5.80U2-103[»]
2Z4LX-ray4.45U2-104[»]
2Z4NX-ray4.45U2-104[»]
3BBXelectron microscopy10.00U2-104[»]
3DF2X-ray3.50U2-103[»]
3DF4X-ray3.50U2-103[»]
3E1Belectron microscopy-O1-103[»]
3E1Delectron microscopy-O1-103[»]
3FIKelectron microscopy6.70U2-103[»]
3I1NX-ray3.19U1-104[»]
3I1PX-ray3.19U1-104[»]
3I1RX-ray3.81U1-104[»]
3I1TX-ray3.81U1-104[»]
3I20X-ray3.71U1-104[»]
3I22X-ray3.71U1-104[»]
3IZTelectron microscopy-V1-104[»]
3IZUelectron microscopy-V1-104[»]
3J01electron microscopy-U2-104[»]
3J0Telectron microscopy12.10W2-104[»]
3J0Welectron microscopy14.70W2-104[»]
3J0Yelectron microscopy13.50W2-104[»]
3J11electron microscopy13.10W2-104[»]
3J12electron microscopy11.50W2-104[»]
3J14electron microscopy11.50W2-104[»]
3J19electron microscopy8.30U2-103[»]
3J37electron microscopy9.80Y2-104[»]
3J45electron microscopy9.50U2-104[»]
3J46electron microscopy10.10U2-104[»]
3J4Xelectron microscopy12.00U1-103[»]
3J50electron microscopy20.00U1-103[»]
3J51electron microscopy17.00U1-103[»]
3J52electron microscopy12.00U1-103[»]
3J54electron microscopy13.00U1-103[»]
3J56electron microscopy15.00U1-103[»]
3J58electron microscopy17.00U1-103[»]
3J5Aelectron microscopy12.00U1-103[»]
3J5Celectron microscopy17.00U1-103[»]
3J5Eelectron microscopy17.00U1-103[»]
3J5Gelectron microscopy20.00U1-103[»]
3J5Ielectron microscopy15.00U1-103[»]
3J5Kelectron microscopy9.00U1-103[»]
3J5Lelectron microscopy6.60U2-103[»]
3J5Oelectron microscopy6.80U1-104[»]
3J5Uelectron microscopy7.60W2-104[»]
3J5Welectron microscopy7.60X2-104[»]
3KCRelectron microscopy-U1-104[»]
3OASX-ray3.25U2-103[»]
3OATX-ray3.25U2-103[»]
3OFCX-ray3.19U2-103[»]
3OFDX-ray3.19U2-103[»]
3OFQX-ray3.10U2-103[»]
3OFRX-ray3.10U2-103[»]
3OFZX-ray3.29U2-103[»]
3OG0X-ray3.29U2-103[»]
3ORBX-ray3.30U1-104[»]
3R8SX-ray3.00U2-103[»]
3R8TX-ray3.00U2-103[»]
3SGFX-ray3.20Y1-104[»]
3UOSX-ray3.70Y1-104[»]
4CSUelectron microscopy5.50U2-104[»]
4GARX-ray3.30U1-104[»]
4GAUX-ray3.30U1-104[»]
4KIXX-ray2.90U1-104[»]
4KIZX-ray2.90U1-104[»]
4KJ1X-ray2.90U1-104[»]
4KJ3X-ray2.90U1-104[»]
4KJ5X-ray2.90U1-104[»]
4KJ7X-ray2.90U1-104[»]
4KJ9X-ray2.90U1-104[»]
4KJBX-ray2.90U1-104[»]
4PEBX-ray2.95U2-103[»]
4PECX-ray2.95U2-103[»]
4TOMX-ray3.00U2-103[»]
4TOOX-ray3.00U2-103[»]
4TOVX-ray2.90U2-103[»]
4TOXX-ray2.90U2-103[»]
4TP1X-ray2.90U2-103[»]
4TP3X-ray2.90U2-103[»]
4TP5X-ray2.90U2-103[»]
4TP7X-ray2.90U2-103[»]
4TP9X-ray2.80U2-103[»]
4TPBX-ray2.80U2-103[»]
4TPDX-ray2.80U2-103[»]
4TPFX-ray2.80U2-103[»]
ProteinModelPortaliP60624.
SMRiP60624. Positions 2-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60624.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L24P family.Curated

Phylogenomic databases

eggNOGiCOG0198.
HOGENOMiHOG000039892.
InParanoidiP60624.
KOiK02895.
OMAiINEHAYL.
OrthoDBiEOG6FFSDM.
PhylomeDBiP60624.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60624-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKIRRDDE VIVLTGKDKG KRGKVKNVLS SGKVIVEGIN LVKKHQKPVP
60 70 80 90 100
ALNQPGGIVE KEAAIQVSNV AIFNAATGKA DRVGFRFEDG KKVRFFKSNS

ETIK
Length:104
Mass (Da):11,316
Last modified:January 23, 2007 - v2
Checksum:i0ABF7DD305FA07F5
GO

Mass spectrometryi

Molecular mass is 11186.5 Da from positions 2 - 104. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25716.1.
U18997 Genomic DNA. Translation: AAA58106.1.
U00096 Genomic DNA. Translation: AAC76334.1.
AP009048 Genomic DNA. Translation: BAE77982.1.
M10195 Genomic DNA. Translation: AAA24050.1.
PIRiH65123. R5EC24.
RefSeqiNP_417768.1. NC_000913.3.
YP_492123.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76334; AAC76334; b3309.
BAE77982; BAE77982; BAE77982.
GeneIDi12934409.
947810.
KEGGiecj:Y75_p3867.
eco:b3309.
PATRICi32122050. VBIEscCol129921_3402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25716.1 .
U18997 Genomic DNA. Translation: AAA58106.1 .
U00096 Genomic DNA. Translation: AAC76334.1 .
AP009048 Genomic DNA. Translation: BAE77982.1 .
M10195 Genomic DNA. Translation: AAA24050.1 .
PIRi H65123. R5EC24.
RefSeqi NP_417768.1. NC_000913.3.
YP_492123.1. 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 u 2-104 [» ]
1P85 electron microscopy 12.30 S 2-104 [» ]
1P86 electron microscopy 11.50 S 2-104 [» ]
1VS6 X-ray 3.46 U 1-104 [» ]
1VS8 X-ray 3.46 U 1-104 [» ]
1VT2 X-ray 3.30 U 1-104 [» ]
2AW4 X-ray 3.46 U 2-104 [» ]
2AWB X-ray 3.46 U 2-104 [» ]
2GYA electron microscopy 15.00 S 4-102 [» ]
2GYC electron microscopy 15.00 S 4-102 [» ]
2I2T X-ray 3.22 U 2-104 [» ]
2I2V X-ray 3.22 U 2-104 [» ]
2J28 electron microscopy 8.00 U 2-103 [» ]
2QAM X-ray 3.21 U 2-104 [» ]
2QAO X-ray 3.21 U 2-104 [» ]
2QBA X-ray 3.54 U 2-104 [» ]
2QBC X-ray 3.54 U 2-104 [» ]
2QBE X-ray 3.30 U 2-104 [» ]
2QBG X-ray 3.30 U 2-104 [» ]
2QBI X-ray 4.00 U 2-104 [» ]
2QBK X-ray 4.00 U 2-104 [» ]
2QOV X-ray 3.93 U 2-104 [» ]
2QOX X-ray 3.93 U 2-104 [» ]
2QOZ X-ray 3.50 U 2-104 [» ]
2QP1 X-ray 3.50 U 2-104 [» ]
2RDO electron microscopy 9.10 U 2-104 [» ]
2VHM X-ray 3.74 U 2-104 [» ]
2VHN X-ray 3.74 U 2-104 [» ]
2VRH electron microscopy 19.00 C 2-104 [» ]
2WWQ electron microscopy 5.80 U 2-103 [» ]
2Z4L X-ray 4.45 U 2-104 [» ]
2Z4N X-ray 4.45 U 2-104 [» ]
3BBX electron microscopy 10.00 U 2-104 [» ]
3DF2 X-ray 3.50 U 2-103 [» ]
3DF4 X-ray 3.50 U 2-103 [» ]
3E1B electron microscopy - O 1-103 [» ]
3E1D electron microscopy - O 1-103 [» ]
3FIK electron microscopy 6.70 U 2-103 [» ]
3I1N X-ray 3.19 U 1-104 [» ]
3I1P X-ray 3.19 U 1-104 [» ]
3I1R X-ray 3.81 U 1-104 [» ]
3I1T X-ray 3.81 U 1-104 [» ]
3I20 X-ray 3.71 U 1-104 [» ]
3I22 X-ray 3.71 U 1-104 [» ]
3IZT electron microscopy - V 1-104 [» ]
3IZU electron microscopy - V 1-104 [» ]
3J01 electron microscopy - U 2-104 [» ]
3J0T electron microscopy 12.10 W 2-104 [» ]
3J0W electron microscopy 14.70 W 2-104 [» ]
3J0Y electron microscopy 13.50 W 2-104 [» ]
3J11 electron microscopy 13.10 W 2-104 [» ]
3J12 electron microscopy 11.50 W 2-104 [» ]
3J14 electron microscopy 11.50 W 2-104 [» ]
3J19 electron microscopy 8.30 U 2-103 [» ]
3J37 electron microscopy 9.80 Y 2-104 [» ]
3J45 electron microscopy 9.50 U 2-104 [» ]
3J46 electron microscopy 10.10 U 2-104 [» ]
3J4X electron microscopy 12.00 U 1-103 [» ]
3J50 electron microscopy 20.00 U 1-103 [» ]
3J51 electron microscopy 17.00 U 1-103 [» ]
3J52 electron microscopy 12.00 U 1-103 [» ]
3J54 electron microscopy 13.00 U 1-103 [» ]
3J56 electron microscopy 15.00 U 1-103 [» ]
3J58 electron microscopy 17.00 U 1-103 [» ]
3J5A electron microscopy 12.00 U 1-103 [» ]
3J5C electron microscopy 17.00 U 1-103 [» ]
3J5E electron microscopy 17.00 U 1-103 [» ]
3J5G electron microscopy 20.00 U 1-103 [» ]
3J5I electron microscopy 15.00 U 1-103 [» ]
3J5K electron microscopy 9.00 U 1-103 [» ]
3J5L electron microscopy 6.60 U 2-103 [» ]
3J5O electron microscopy 6.80 U 1-104 [» ]
3J5U electron microscopy 7.60 W 2-104 [» ]
3J5W electron microscopy 7.60 X 2-104 [» ]
3KCR electron microscopy - U 1-104 [» ]
3OAS X-ray 3.25 U 2-103 [» ]
3OAT X-ray 3.25 U 2-103 [» ]
3OFC X-ray 3.19 U 2-103 [» ]
3OFD X-ray 3.19 U 2-103 [» ]
3OFQ X-ray 3.10 U 2-103 [» ]
3OFR X-ray 3.10 U 2-103 [» ]
3OFZ X-ray 3.29 U 2-103 [» ]
3OG0 X-ray 3.29 U 2-103 [» ]
3ORB X-ray 3.30 U 1-104 [» ]
3R8S X-ray 3.00 U 2-103 [» ]
3R8T X-ray 3.00 U 2-103 [» ]
3SGF X-ray 3.20 Y 1-104 [» ]
3UOS X-ray 3.70 Y 1-104 [» ]
4CSU electron microscopy 5.50 U 2-104 [» ]
4GAR X-ray 3.30 U 1-104 [» ]
4GAU X-ray 3.30 U 1-104 [» ]
4KIX X-ray 2.90 U 1-104 [» ]
4KIZ X-ray 2.90 U 1-104 [» ]
4KJ1 X-ray 2.90 U 1-104 [» ]
4KJ3 X-ray 2.90 U 1-104 [» ]
4KJ5 X-ray 2.90 U 1-104 [» ]
4KJ7 X-ray 2.90 U 1-104 [» ]
4KJ9 X-ray 2.90 U 1-104 [» ]
4KJB X-ray 2.90 U 1-104 [» ]
4PEB X-ray 2.95 U 2-103 [» ]
4PEC X-ray 2.95 U 2-103 [» ]
4TOM X-ray 3.00 U 2-103 [» ]
4TOO X-ray 3.00 U 2-103 [» ]
4TOV X-ray 2.90 U 2-103 [» ]
4TOX X-ray 2.90 U 2-103 [» ]
4TP1 X-ray 2.90 U 2-103 [» ]
4TP3 X-ray 2.90 U 2-103 [» ]
4TP5 X-ray 2.90 U 2-103 [» ]
4TP7 X-ray 2.90 U 2-103 [» ]
4TP9 X-ray 2.80 U 2-103 [» ]
4TPB X-ray 2.80 U 2-103 [» ]
4TPD X-ray 2.80 U 2-103 [» ]
4TPF X-ray 2.80 U 2-103 [» ]
ProteinModelPortali P60624.
SMRi P60624. Positions 2-103.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47846N.
IntActi P60624. 51 interactions.
MINTi MINT-1294921.
STRINGi 511145.b3309.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P60624.
PRIDEi P60624.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76334 ; AAC76334 ; b3309 .
BAE77982 ; BAE77982 ; BAE77982 .
GeneIDi 12934409.
947810.
KEGGi ecj:Y75_p3867.
eco:b3309.
PATRICi 32122050. VBIEscCol129921_3402.

Organism-specific databases

EchoBASEi EB0877.
EcoGenei EG10884. rplX.

Phylogenomic databases

eggNOGi COG0198.
HOGENOMi HOG000039892.
InParanoidi P60624.
KOi K02895.
OMAi INEHAYL.
OrthoDBi EOG6FFSDM.
PhylomeDBi P60624.

Enzyme and pathway databases

BioCyci EcoCyc:EG10884-MONOMER.
ECOL316407:JW3271-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60624.
PROi P60624.

Gene expression databases

Genevestigatori P60624.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
HAMAPi MF_01326_B. Ribosomal_L24_B.
InterProi IPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view ]
PANTHERi PTHR12903. PTHR12903. 1 hit.
Pfami PF00467. KOW. 1 hit.
[Graphical view ]
SMARTi SM00739. KOW. 1 hit.
[Graphical view ]
SUPFAMi SSF50104. SSF50104. 1 hit.
TIGRFAMsi TIGR01079. rplX_bact. 1 hit.
PROSITEi PS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Primary structure of protein L24 from the Escherichia coli ribosome."
    Wittmann-Liebold B.
    FEBS Lett. 108:75-80(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-104.
    Strain: K12.
  5. "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA."
    Olins P.O., Nomura M.
    Nucleic Acids Res. 9:1757-1764(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-104.
    Strain: K12 / JM105 / ATCC 47016.
  6. "The ribosomal protein L24 of Escherichia coli is an assembly protein."
    Spillmann S., Nierhaus K.H.
    J. Biol. Chem. 253:7047-7050(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUBUNIT ASSEMBLY.
    Strain: K12 / A19.
  7. "Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes."
    Nowotny V., Nierhaus K.H.
    Proc. Natl. Acad. Sci. U.S.A. 79:7238-7242(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS AN ASSEMBLY INITIATOR PROTEIN.
  8. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  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. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
    Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
    Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
    Strain: MRE-600.
  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).
    Strain: MRE-600.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL24_ECOLI
AccessioniPrimary (citable) accession number: P60624
Secondary accession number(s): P02425, P37438, Q2M6X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 119 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